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[[Image:1ibw.jpg|left|200px]]


{{Structure
==STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT 25 C==
|PDB= 1ibw |SIZE=350|CAPTION= <scene name='initialview01'>1ibw</scene>, resolution 3.2&Aring;
<StructureSection load='1ibw' size='340' side='right'caption='[[1ibw]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>
<table><tr><td colspan='2'>[[1ibw]] 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=1IBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBW FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
|GENE= HDCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1591 Lactobacillus sp.])
<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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ibw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibw OCA], [https://pdbe.org/1ibw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibw RCSB], [https://www.ebi.ac.uk/pdbsum/1ibw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibw ProSAT]</span></td></tr>
|RELATEDENTRY=[[1pya|1PYA]], [[1hq6|1HQ6]], [[1ibt|1IBT]], [[1ibu|1IBU]], [[1ibv|1IBV]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ibw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibw OCA], [http://www.ebi.ac.uk/pdbsum/1ibw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibw RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/DCHS_LACS3 DCHS_LACS3]
 
== Evolutionary Conservation ==
'''STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT 25 C'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ibw_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1IBW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBW OCA].  
</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=1ibw ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
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://www.ncbi.nlm.nih.gov/pubmed/11835507 11835507]
</StructureSection>
[[Category: Histidine decarboxylase]]
[[Category: Lactobacillus sp. 30A]]
[[Category: Lactobacillus sp.]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Ernst S]]
[[Category: Ernst, S.]]
[[Category: Monzingo AF]]
[[Category: Monzingo, A F.]]
[[Category: Robertus JD]]
[[Category: Robertus, J D.]]
[[Category: Schelp E]]
[[Category: Schelp, E.]]
[[Category: Worley S]]
[[Category: Worley, S.]]
[[Category: active form]]
[[Category: carboxy-lyase]]
[[Category: pyruvoyl]]
[[Category: site-directed mutant]]
[[Category: substrate-induced activation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:34 2008''
Retrieved from "https://proteopedia.org/1ibw"