2zk9

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Current revision (08:38, 7 February 2024) (edit) (undo)
 
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<StructureSection load='2zk9' size='340' side='right'caption='[[2zk9]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='2zk9' size='340' side='right'caption='[[2zk9]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2zk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"chryseobacterium_proteolyticum"_yamaguchi_and_yokoe_2000 "chryseobacterium proteolyticum" yamaguchi and yokoe 2000]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z8t 2z8t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZK9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2zk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chryseobacterium_proteolyticum Chryseobacterium proteolyticum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z8t 2z8t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZK9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a54|3a54]], [[3a55|3a55]], [[3a56|3a56]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2zk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zk9 OCA], [https://pdbe.org/2zk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zk9 RCSB], [https://www.ebi.ac.uk/pdbsum/2zk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zk9 ProSAT]</span></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=2zk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zk9 OCA], [https://pdbe.org/2zk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zk9 RCSB], [https://www.ebi.ac.uk/pdbsum/2zk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zk9 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9AQQ8_9FLAO Q9AQQ8_9FLAO]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2zk9" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glutaminase 3D structures|Glutaminase 3D structures]]
*[[Glutaminase 3D structures|Glutaminase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chryseobacterium proteolyticum yamaguchi and yokoe 2000]]
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[[Category: Chryseobacterium proteolyticum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hashizume, R]]
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[[Category: Hashizume R]]
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[[Category: Deamidation glutaminase]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of Protein-glutaminase

PDB ID 2zk9

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