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| | <StructureSection load='1hq6' size='340' side='right'caption='[[1hq6]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1hq6' size='340' side='right'caption='[[1hq6]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hq6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacs3 Lacs3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1HQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hq6]] is a 4 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=1HQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQ6 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pya|1pya]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1593 LACS3])</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=1hq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hq6 OCA], [https://pdbe.org/1hq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hq6 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1hq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hq6 OCA], [http://pdbe.org/1hq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hq6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DCHS_LACS3 DCHS_LACS3] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine decarboxylase]] | + | [[Category: Lactobacillus sp. 30A]] |
| - | [[Category: Lacs3]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ernst, S]] | + | [[Category: Ernst S]] |
| - | [[Category: Monzingo, A F]] | + | [[Category: Monzingo AF]] |
| - | [[Category: Robertus, J D]] | + | [[Category: Robertus JD]] |
| - | [[Category: Schelp, E]] | + | [[Category: Schelp E]] |
| - | [[Category: Worley, S]] | + | [[Category: Worley S]] |
| - | [[Category: Carboxy-lyase]]
| + | |
| - | [[Category: Helix disorder]]
| + | |
| - | [[Category: Less active form]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Ph regulation]]
| + | |
| - | [[Category: Pyruvoyl]]
| + | |
| Structural highlights
Function
DCHS_LACS3
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.
pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.,Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD J Mol Biol. 2001 Mar 2;306(4):727-32. PMID:11243783[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD. pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. J Mol Biol. 2001 Mar 2;306(4):727-32. PMID:11243783 doi:10.1006/jmbi.2000.4430
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