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3a55
From Proteopedia
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| - | [[ | + | ==Crystal structure of the A47Q2 mutant of pro- protein-glutaminase== |
| + | <StructureSection load='3a55' size='340' side='right' caption='[[3a55]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3a55]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chryseobacterium_proteolyticum Chryseobacterium proteolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A55 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zk9|2zk9]], [[3a54|3a54]], [[3a56|3a56]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=118127 Chryseobacterium proteolyticum])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a55 RCSB], [http://www.ebi.ac.uk/pdbsum/3a55 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | ||
| - | + | ==See Also== | |
| - | + | *[[Glutaminase|Glutaminase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Chryseobacterium proteolyticum]] | [[Category: Chryseobacterium proteolyticum]] | ||
[[Category: Hashizume, R.]] | [[Category: Hashizume, R.]] | ||
Revision as of 06:58, 9 June 2014
Crystal structure of the A47Q2 mutant of pro- protein-glutaminase
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