1ibt: Difference between revisions

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-{{Seed}}
-[[Image:1ibt.png|left|200px]]
-<!--
+==STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C==
-The line below this paragraph, containing "STRUCTURE_1ibt", creates the "Structure Box" on the page.
+<StructureSection load='1ibt' size='340' side='right'caption='[[1ibt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ibt]] 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=1IBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBT FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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>
-{{STRUCTURE_1ibt|  PDB=1ibt  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ibt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibt OCA], [https://pdbe.org/1ibt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibt RCSB], [https://www.ebi.ac.uk/pdbsum/1ibt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibt 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/ib/1ibt_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=1ibt ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C===
+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:11835507<ref>PMID:11835507</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11835507}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ibt" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11835507 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11835507}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Lactobacillus sp. 30A]]
-IBT is a 6 chains 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=1IBT OCA].
+[[Category: Large Structures]]
+[[Category: Ernst S]]
-==Reference==
+[[Category: Monzingo AF]]
-<ref group="xtra">PMID:11835507</ref><references group="xtra"/>
+[[Category: Robertus JD]]
-[[Category: Histidine decarboxylase]]
+[[Category: Schelp E]]
-[[Category: Lactobacillus sp.]]
+[[Category: Worley S]]
-[[Category: Ernst, S.]]
-[[Category: Monzingo, A F.]]
-[[Category: Robertus, J D.]]
-[[Category: Schelp, E.]]
-[[Category: Worley, S.]]
-[[Category: Carboxy-lyase]]
-[[Category: Helix disorder]]
-[[Category: Less active form]]
-[[Category: Pyruvoyl]]
-[[Category: Site-directed mutant]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:46:16 2009''