Protein Family Models

collagen-like triple helix repeat-containing protein may be a surface protein

Date:

2024-02-09

collagen-like triple helix repeat-containing protein may be a surface protein

Date:

2024-02-09

collagen-like triple helix repeat-containing protein may be a surface protein

Date:

2024-02-09

M14 family zinc carboxypeptidase N/E relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; also contains C-terminal collagen triple helix repeat domain

Date:

2024-02-09

This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks residues in these lectins identified as binding carbohydrates. The beta-prism and beta-sandwich domains reinforce overall trimeric assembly and therefore may have indirect roles in stabilizing the backbone of the variable region [1]. [1]. 16170324. The C-type lectin fold as an evolutionary solution for massive. sequence variation.. McMahon SA, Miller JL, Lawton JA, Kerkow DE, Hodes A,. Marti-Renom MA, Doulatov S, Narayanan E, Sali A, Miller JF,. Ghosh P;. Nat Struct Mol Biol. 2005;12:886-892.. [2]. 18532877. Selective ligand recognition by a diversity-generating. retroelement variable protein.. Miller JL, Le Coq J, Hodes A, Barbalat R, Miller JF, Ghosh P;. PLoS Biol. 2008;6:e131.. [3]. 16314578. Structure of a group A streptococcal phage-encoded virulence. factor reveals a catalytically active triple-stranded. beta-helix.. Smith NL, Taylor EJ, Lindsay AM, Charnock SJ, Turkenburg JP,. Dodson EJ, Davies GJ, Black GW;. Proc Natl Acad Sci U S A. 2005;102:17652-17657.. [4]. 19438710. Polysaccharide binding sites in hyaluronate lyase--crystal. structures of native phage-encoded hyaluronate lyase and its. complexes with ascorbic acid and lactose.. Mishra P, Prem Kumar R, Ethayathulla AS, Singh N, Sharma S,. Perbandt M, Betzel C, Kaur P, Srinivasan A, Bhakuni V, Singh TP;. FEBS J. 2009;276:3392-3402. (from Pfam)

Date:

2024-08-14

Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) Pfam:PF00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat [1]. [1]. 21536047. Crystal structure of a rigid four-spectrin-repeat fragment of. the human desmoplakin plakin domain.. Choi HJ, Weis WI;. J Mol Biol. 2011;409:800-812. (from Pfam)

Date:

2024-08-14

Collagen_mid is the conserved central region of bacterial collagen triple helix repeat proteins. [1]. 11158359. Streptococcus pyogenes sclB encodes a putative hypervariable. surface protein with a collagen-like repetitive structure.. Whatmore AM;. Microbiology. 2001;147:419-429.. [2]. 21726633. Characterisation of a large family of polymorphic collagen-like. proteins in the endospore-forming bacterium Pasteuria ramosa.. McElroy K, Mouton L, Du Pasquier L, Qi W, Ebert D;. Res Microbiol. 2011;162:701-714. (from Pfam)

Date:

2024-08-14

Members of this family adopt a right-handed triple-stranded beta-helix fold, and are found in the middle of the phage short tail fibre protein gp12 [1]. [1]. 11743729. Crystal structure of a heat and protease-stable part of the. bacteriophage T4 short tail fibre.. van Raaij MJ, Schoehn G, Burda MR, Miller S;. J Mol Biol. 2001;314:1137-1146. (from Pfam)

Date:

2024-08-14

This domain family is found in bacteria and viruses, and is approximately 160 amino acids in length. There are two conserved sequence motifs: VSR and YGA. This domain is the C terminal domain of the bacteriophage protein endosialidase. The endosialidase protein forms homotrimeric molecules and this domain complexes into a tail-spike stalk. The stalk region folds in a triple beta-helix that is interrupted by a small triple beta-prism domain. The tail-spike is a multifunctional protein device used by the phage to fulfill the following functions: (i) to adsorb to the bacterial polySia capsule (ii) to de-polymerise the capsule to gain access to the outer bacterial membrane, and finally (iii) to mediate tight adhesion to the membrane, a prerequisite for the initiation of the infection cycle. [1]. 15608653. Crystal structure of the polysialic acid-degrading endosialidase. of bacteriophage K1F.. Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner. R;. Nat Struct Mol Biol. 2005;12:90-96. (from Pfam)

Date:

2024-08-14

This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes. [1]. 10843861. Core structure of the outer membrane lipoprotein from. Escherichia coli at 1.9 A resolution.. Shu W, Liu J, Ji H, Lu M;. J Mol Biol. 2000;299:1101-1112.. [2]. 12054830. Core side-chain packing and backbone conformation in Lpp-56. coiled-coil mutants.. Liu J, Cao W, Lu M;. J Mol Biol. 2002;318:877-888.. [3]. 12741822. Zinc-mediated helix capping in a triple-helical protein.. Liu J, Dai J, Lu M;. Biochemistry. 2003;42:5657-5664.. [4]. 15520380. Atomic structure of a tryptophan-zipper pentamer.. Liu J, Yong W, Deng Y, Kallenbach NR, Lu M;. Proc Natl Acad Sci U S A. 2004;101:16156-16161.. [5]. 16828114. Conformational transition between four and five-stranded. phenylalanine zippers determined by a local packing interaction.. Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M;. J Mol Biol. 2006;361:168-179. (from Pfam)

Date:

2024-08-14

Delta atracotoxin produces potentially fatal neurotoxic symptoms in primates by slowing he inactivation of voltage-gated sodium channels [1]. The structure of atracotoxin comprises a core beta region containing a triple-stranded a thumb-like extension protruding from the beta region and a C-terminal helix. The beta region contains a cystine knot motif, a feature seen in other neurotoxic polypeptides [1]. [1]. 9384567. The structure of versutoxin (delta-atracotoxin-Hv1) provides. insights into the binding of site 3 neurotoxins to the. voltage-gated sodium channel.. Fletcher JI, Chapman BE, Mackay JP, Howden ME, King GF;. Structure 1997;5:1525-1535. (from Pfam)

Date:

2024-08-14

This small triple helical domain has been predicted to assume a topology similar to helix-turn-helix domains. These domains are found at the C-terminus of proteins related to Swiss:P32157 [1,2]. See figure 2.. [1]. 11886751. MOSC domains: ancient, predicted sulfur-carrier domains, present. in diverse metal--sulfur cluster biosynthesis proteins including. Molybdenum cofactor sulfurases.. Anantharaman V, Aravind L;. FEMS Microbiol Lett 2002;207:55-61.. [2]. 29459651. Crystal structure of the hydroxylaminopurine resistance protein,. YiiM, and its putative molybdenum cofactor-binding catalytic. site.. Namgung B, Kim JH, Song WS, Yoon SI;. Sci Rep. 2018;8:3304. (from Pfam)

Date:

2024-08-14

Members of this family belong to the collagen superfamily [1]. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins [2,3]. [1]. 8240831. New members of the collagen superfamily. Mayne R, Brewton RG;. Curr Opin Cell Biol 1993;5:883-890.. [2]. 11158359. Streptococcus pyogenes sclB encodes a putative hypervariable. surface protein with a collagen-like repetitive structure.. Whatmore AM;. Microbiology. 2001;147:419-429.. [3]. 21726633. Characterisation of a large family of polymorphic collagen-like. proteins in the endospore-forming bacterium Pasteuria ramosa.. McElroy K, Mouton L, Du Pasquier L, Qi W, Ebert D;. Res Microbiol. 2011;162:701-714. (from Pfam)

Date:

2024-08-14

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Date:

2023-12-20

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

Date:

2023-12-19

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Date:

2022-10-12

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Date:

2024-06-20

collagen-like protein similar to collagen, a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Date:

2022-06-08

Members of this family have an exosporium leader peptide-containing N-terminal region, an extensive collagen triple helix-related covering most of the length of the protein, and a BclA-related C-terminal domain. Lengths are variable.

Date:

2023-02-10

collagen-like protein similar to collagen, a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Date:

2021-03-16