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| | ==Crystal structure of pro- protein-glutaminase== | | ==Crystal structure of pro- protein-glutaminase== |
| - | <StructureSection load='3a56' size='340' side='right' caption='[[3a56]], [[Resolution|resolution]] 1.73Å' scene=''> | + | <StructureSection load='3a56' size='340' side='right'caption='[[3a56]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"chryseobacterium_proteolyticum"_yamaguchi_and_yokoe_2000 "chryseobacterium proteolyticum" yamaguchi and yokoe 2000]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A56 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zk9|2zk9]], [[3a54|3a54]], [[3a55|3a55]]</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='gene'><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" Yamaguchi and Yokoe 2000])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a56 OCA], [http://pdbe.org/3a56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a56 RCSB], [http://www.ebi.ac.uk/pdbsum/3a56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a56 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9AQQ8_9FLAO Q9AQQ8_9FLAO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Glutaminase|Glutaminase]] | + | *[[Glutaminase 3D structures|Glutaminase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chryseobacterium proteolyticum yamaguchi and yokoe 2000]] | + | [[Category: Chryseobacterium proteolyticum]] |
| - | [[Category: Hashizume, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Mikami, B]] | + | [[Category: Hashizume R]] |
| - | [[Category: Yamaguchi, S]] | + | [[Category: Mikami B]] |
| - | [[Category: Hydrolase]] | + | [[Category: Yamaguchi S]] |
| - | [[Category: Pro-enzyme]]
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| Structural highlights
Function
Q9AQQ8_9FLAO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hashizume R, Maki Y, Mizutani K, Takahashi N, Matsubara H, Sugita A, Sato K, Yamaguchi S, Mikami B. Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex. J Biol Chem. 2011 Nov 4;286(44):38691-702. Epub 2011 Sep 16. PMID:21926168 doi:10.1074/jbc.M111.255133
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