3abn: Difference between revisions
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New page: '''Unreleased structure''' The entry 3abn is ON HOLD Authors: Okuyama, K., Shimura, M, Kawaguchi, T., Noguchi, K., Mizuno, K., Bachinger, H. P. Description: Crystal structure of (Pro-P... |
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The | ==Crystal structure of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.02 A== | ||
<StructureSection load='3abn' size='340' side='right'caption='[[3abn]], [[Resolution|resolution]] 1.02Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3abn]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ABN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ABN 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]] 1.02Å</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=3abn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3abn OCA], [https://pdbe.org/3abn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3abn RCSB], [https://www.ebi.ac.uk/pdbsum/3abn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3abn ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The single-crystal structure of the collagen-like peptide (Pro-Pro-Gly)4 -Hyp-Asp-Gly-(Pro-Pro-Gly)4 , was analyzed at 1.02 A resolution. The overall average helical twist (theta = 49.6 degrees ) suggests that this peptide adopts a 7/2 triple-helical structure and that its conformation is very similar to that of (Gly-Pro-Hyp)9 , which has the typical repeating sequence in collagen. High-resolution studies on other collagen-like peptides have shown that imino acid-rich sequences preferentially adopt a 7/2 triple-helical structure (theta = 51.4 degrees ), whereas imino acid-lean sequences adopt relaxed conformations (theta < 51.4 degrees ). The guest Gly-Hyp-Asp sequence in the present peptide, however, has a large helical twist (theta = 61.1 degrees ), whereas that of the host Pro-Pro-Gly sequence is small (theta = 46.7 degrees ), indicating that the relationship between the helical conformation and the amino acid sequence of such peptides is complex. In the present structure, a strong intermolecular hydrogen bond between two Asp residues on the A and B strands might induce the large helical twist of the guest sequence; this is compensated by a reduced helical twist in the host, so that an overall 7/2-helical symmetry is maintained. The Asp residue in the C strand might interact electrostatically with the N-terminus of an adjacent molecule, causing axial displacement, reminiscent of the D-staggered structure in fibrous collagens. (c) 2013 Wiley Periodicals, Inc. Biopolymers 99: 436-447, 2013. | |||
Crystal structure of the collagen model peptide (Pro-Pro-Gly)4 -Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.0 A resolution.,Okuyama K, Kawaguchi T, Shimura M, Noguchi K, Mizuno K, Bachinger HP Biopolymers. 2013 Jul;99(7):436-47. doi: 10.1002/bip.22198. PMID:23616212<ref>PMID:23616212</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3abn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Bachinger HP]] | |||
[[Category: Kawaguchi T]] | |||
[[Category: Mizuno K]] | |||
[[Category: Noguchi K]] | |||
[[Category: Okuyama K]] | |||
[[Category: Shimura M]] | |||
Latest revision as of 22:31, 26 March 2025
Crystal structure of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 at 1.02 A
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