3k8z
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3k8z is ON HOLD Authors: Gunka, K, Newman, J.A., Commichau, F.M., Herzberg, C., Rodrigues, C., Hewitt, L., Lewis, R.J., Stulke, J. Description: Cry...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Gudb1 a decryptified secondary glutamate dehydrogenase from B. subtilis== | |
| + | <StructureSection load='3k8z' size='340' side='right'caption='[[3k8z]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3k8z]] is a 6 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=3K8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K8Z 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]] 2.4Å</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=3k8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k8z OCA], [https://pdbe.org/3k8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k8z RCSB], [https://www.ebi.ac.uk/pdbsum/3k8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k8z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GUDB_BACSU GUDB_BACSU] GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate.<ref>PMID:9829940</ref> <ref>PMID:18326565</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/3k8z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3k8z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Commichau FM]] | ||
| + | [[Category: Gunka K]] | ||
| + | [[Category: Herzberg C]] | ||
| + | [[Category: Hewitt L]] | ||
| + | [[Category: Lewis RJ]] | ||
| + | [[Category: Newman JA]] | ||
| + | [[Category: Rodrigues C]] | ||
| + | [[Category: Stulke J]] | ||
Current revision
Crystal Structure of Gudb1 a decryptified secondary glutamate dehydrogenase from B. subtilis
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Categories: Bacillus subtilis | Large Structures | Commichau FM | Gunka K | Herzberg C | Hewitt L | Lewis RJ | Newman JA | Rodrigues C | Stulke J
