1hq6
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1hq6.jpg|left|200px]]<br /><applet load="1hq6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hq6, resolution 2.7Å" /> | ||
| - | '''STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8'''<br /> | ||
| - | == | + | ==STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8== |
| + | <StructureSection load='1hq6' size='340' side='right'caption='[[1hq6]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DCHS_LACS3 DCHS_LACS3] | ||
| + | == 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/hq/1hq6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1hq6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | 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<ref>PMID:11243783</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1hq6" style="background-color:#fffaf0;"></div> | |
| - | [[Category: Lactobacillus sp.]] | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Ernst | + | __TOC__ |
| - | [[Category: Monzingo | + | </StructureSection> |
| - | [[Category: Robertus | + | [[Category: Lactobacillus sp. 30A]] |
| - | [[Category: Schelp | + | [[Category: Large Structures]] |
| - | [[Category: Worley | + | [[Category: Ernst S]] |
| - | + | [[Category: Monzingo AF]] | |
| - | + | [[Category: Robertus JD]] | |
| - | + | [[Category: Schelp E]] | |
| - | + | [[Category: Worley S]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8
| |||||||||||
