3b0s: Difference between revisions
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==Crystal Structure of (Gly-Pro-Hyp)9== | |||
<StructureSection load='3b0s' size='340' side='right'caption='[[3b0s]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3b0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saimiriine_gammaherpesvirus_2 Saimiriine gammaherpesvirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B0S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0s OCA], [https://pdbe.org/3b0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b0s RCSB], [https://www.ebi.ac.uk/pdbsum/3b0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b0s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q80BK4_SHV2 Q80BK4_SHV2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Collagens have long been believed to adopt a triple-stranded molecular structure with a 10/3 symmetry (ten triplet units in three turns) and an axial repeat of 29 A. This belief even persisted after an alternative structure with a 7/2 symmetry (seven triplet units in two turns) with an axial repeat of 20 A had been proposed. The uncertainty regarding the helical symmetry of collagens is attributed to inadequate X-ray fiber diffraction data. Therefore, for better understanding of the collagen helix, single-crystal analyses of peptides with simplified characteristic amino acid sequences and similar compositions to collagens have long been awaited. Here we report the crystal structure of (Gly-Pro-Hyp)(9) peptide at a resolution of 1.45 A. The repeating unit of this peptide, Gly-Pro-Hyp, is the most typical sequence present in collagens, and it has been used as a basic repeating unit in fiber diffraction analyses of collagen. The (Gly-Pro-Hyp)(9) peptide adopts a triple-stranded structure with an average helical symmetry close to the ideal 7/2 helical model for collagen. This observation strongly suggests that the average molecular structure of collagen is not the accepted Rich and Crick 10/3 helical model but is a 7/2 helical conformation. (c) 2012 Wiley Periodicals, Inc. Biopolymers 97: 607-616, 2012. | |||
Crystal structure of (Gly-Pro-Hyp)(9) : Implications for the collagen molecular model.,Okuyama K, Miyama K, Mizuno K, Bachinger HP Biopolymers. 2012 Aug;97(8):607-16. doi: 10.1002/bip.22048. PMID:22605552<ref>PMID:22605552</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3b0s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saimiriine gammaherpesvirus 2]] | |||
[[Category: Bachinger HP]] | |||
[[Category: Miyama K]] | |||
[[Category: Mizuno K]] | |||
[[Category: Okuyama K]] | |||
