5gyl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:48, 6 November 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5gyl is ON HOLD until Paper Publication
+
==Structure of Cicer arietinum 11S gloubulin==
 +
<StructureSection load='5gyl' size='340' side='right'caption='[[5gyl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5gyl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cicer_arietinum Cicer arietinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GYL 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]] 2.2&#8491;</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=5gyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gyl OCA], [https://pdbe.org/5gyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gyl RCSB], [https://www.ebi.ac.uk/pdbsum/5gyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gyl ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Chickpea is a crop that is known as a source of high-quality proteins. CL-AI, which belongs to the 11S globulin and cupin superfamily, was initially identified in chickpea seeds. CL-AI has recently been shown to inhibit various types of alpha-amylases. To determine its molecular mechanism, the crystal structure of CL-AI was solved at a final resolution of 2.2 A. Structural analysis indicated that each asymmetric unit contains three molecules with threefold symmetry and a head-to-tail association, and each molecule is divided into an alpha-chain and a beta-chain. CL-AI has high structural similarity to other 11S globulins and canonical metal-dependent enzyme-related cupin proteins, whereas its stimilarity to alpha-amylase inhibitor from Phaseolus vulgaris is quite low. The structure presented here will provide insight into the function of CL-AI.
-
Authors:
+
Crystallization and crystallographic studies of a novel chickpea 11S globulin.,Sun L, Zhou A, Zhang F Acta Crystallogr F Struct Biol Commun. 2022 Sep 1;78(Pt 9):324-329. doi: , 10.1107/S2053230X22007919. Epub 2022 Aug 22. PMID:36048082<ref>PMID:36048082</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5gyl" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Cicer arietinum]]
 +
[[Category: Large Structures]]
 +
[[Category: Zhang F]]
 +
[[Category: Zhou A]]

Current revision

Structure of Cicer arietinum 11S gloubulin

PDB ID 5gyl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools