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1ibv

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(New page: 200px<br /><applet load="1ibv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ibv, resolution 2.5&Aring;" /> '''STRUCTURE OF THE D53,...)
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[[Image:1ibv.jpg|left|200px]]<br /><applet load="1ibv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ibv, resolution 2.5&Aring;" />
 
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'''STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C'''<br />
 
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==Overview==
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==STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C==
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Histidine decarboxylase (HDC) from Lactobacillus 30a converts histidine to, histamine, a process that enables the bacteria to maintain the optimum pH, range for cell growth. HDC is regulated by pH; it is active at low pH and, inactive at neutral to alkaline pH. The X-ray structure of HDC at pH 8, revealed that a helix was disordered, resulting in the disruption of the, substrate-binding site. The HDC trimer has also been shown to exhibit, cooperative kinetics at neutral pH, that is, histidine can trigger a, T-state to R-state transition. The D53,54N mutant of HDC has an elevated, Km, even at low pH, indicating that the enzyme assumes the low activity, T-state. We have solved the structures of the D53,54N mutant at low pH, with and without the substrate analog histidine methyl ester (HME) bound., Structural analysis shows that the apo-D53,54N mutant is in the inactive, or T-state and that binding of the substrate analog induces the enzyme to, adopt the active or R-state. A mechanism for the cooperative transition is, proposed.
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<StructureSection load='1ibv' size='340' side='right'caption='[[1ibv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ibv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_sp._30A Lactobacillus sp. 30A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBV FirstGlance]. <br>
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1IBV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.] with PVH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histidine_decarboxylase Histidine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.22 4.1.1.22] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IBV OCA].
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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]] 2.5&#8491;</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=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ibv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibv OCA], [https://pdbe.org/1ibv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibv RCSB], [https://www.ebi.ac.uk/pdbsum/1ibv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibv ProSAT]</span></td></tr>
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Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a., Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD, Proteins. 2002 Feb 15;46(3):321-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11835507 11835507]
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</table>
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[[Category: Histidine decarboxylase]]
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== Function ==
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[[Category: Lactobacillus sp.]]
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[https://www.uniprot.org/uniprot/DCHS_LACS3 DCHS_LACS3]
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[[Category: Protein complex]]
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== Evolutionary Conservation ==
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[[Category: Ernst, S.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Monzingo, A.F.]]
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Check<jmol>
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[[Category: Robertus, J.D.]]
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<jmolCheckbox>
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[[Category: Schelp, E.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ibv_consurf.spt"</scriptWhenChecked>
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[[Category: Worley, S.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: PVH]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: active form]]
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</jmolCheckbox>
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[[Category: carboxy-lyase]]
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</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=1ibv ConSurf].
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[[Category: pyruvoyl]]
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<div style="clear:both"></div>
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[[Category: site-directed mutant]]
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__TOC__
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[[Category: substrate-induced activation]]
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</StructureSection>
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[[Category: Lactobacillus sp. 30A]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:16:19 2007''
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[[Category: Large Structures]]
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[[Category: Ernst S]]
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[[Category: Monzingo AF]]
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[[Category: Robertus JD]]
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[[Category: Schelp E]]
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[[Category: Worley S]]

Current revision

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C

PDB ID 1ibv

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