3a56: Difference between revisions
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New page: '''Unreleased structure''' The entry 3a56 is ON HOLD Authors: Hashizume, R., Yamaguchi, S., Mikami, B. Description: crystal structure of pro-protein-glutaminase ''Page seeded by [http... |
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The | ==Crystal structure of pro- protein-glutaminase== | ||
<StructureSection load='3a56' size='340' side='right'caption='[[3a56]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3a56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chryseobacterium_proteolyticum Chryseobacterium proteolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A56 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]] 1.728Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=3a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a56 OCA], [https://pdbe.org/3a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a56 RCSB], [https://www.ebi.ac.uk/pdbsum/3a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a56 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9AQQ8_9FLAO Q9AQQ8_9FLAO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein glutaminase, which converts a protein glutamine residue to a glutamate residue, is expected to be useful as a new food-processing enzyme. The crystal structures of the mature and pro forms of the enzyme were refined at 1.15 and 1.73 A resolution, respectively. The overall structure of the mature enzyme has a weak homology to the core domain of human transglutaminase-2. The catalytic triad (Cys-His-Asp) common to transglutaminases and cysteine proteases is located in the bottom of the active site pocket. The structure of the recombinant pro form shows that a short loop between S2 and S3 in the proregion covers and interacts with the active site of the mature region, mimicking the protein substrate of the enzyme. Ala-47 is located just above the pocket of the active site. Two mutant structures (A47Q-1 and A47Q-2) refined at 1.5 A resolution were found to correspond to the enzyme-substrate complex and an S-acyl intermediate. Based on these structures, the catalytic mechanism of protein glutaminase is proposed. | |||
Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex.,Hashizume R, Maki Y, Mizutani K, Takahashi N, Matsubara H, Sugita A, Sato K, Yamaguchi S, Mikami B J Biol Chem. 2011 Nov 4;286(44):38691-702. Epub 2011 Sep 16. PMID:21926168<ref>PMID:21926168</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3a56" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glutaminase 3D structures|Glutaminase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chryseobacterium proteolyticum]] | |||
[[Category: Large Structures]] | |||
[[Category: Hashizume R]] | |||
[[Category: Mikami B]] | |||
[[Category: Yamaguchi S]] | |||
