1qd9
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1qd9' size='340' side='right'caption='[[1qd9]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1qd9' size='340' side='right'caption='[[1qd9]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1qd9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1qd9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QD9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 1.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=1qd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd9 OCA], [https://pdbe.org/1qd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd9 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=1qd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd9 OCA], [https://pdbe.org/1qd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RIDA_BACSU RIDA_BACSU] Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis. May have a role in the purine metabolism.<ref>PMID:22094463</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qd9 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qd9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The yabJ gene in Bacillus subtilis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein. The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7-A crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity. The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins. | ||
| - | |||
| - | Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family.,Sinha S, Rappu P, Lange SC, Mantsala P, Zalkin H, Smith JL Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13074-9. PMID:10557275<ref>PMID:10557275</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1qd9" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Lange | + | [[Category: Lange SC]] |
| - | [[Category: Mantsala | + | [[Category: Mantsala P]] |
| - | [[Category: Rappu | + | [[Category: Rappu P]] |
| - | [[Category: Sinha | + | [[Category: Sinha S]] |
| - | [[Category: Smith | + | [[Category: Smith JL]] |
| - | [[Category: Zalkin | + | [[Category: Zalkin H]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Bacillus subtilis YABJ
| |||||||||||
Categories: Bacillus subtilis | Large Structures | Lange SC | Mantsala P | Rappu P | Sinha S | Smith JL | Zalkin H
