2h9c: Difference between revisions

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-[[Image:2h9c.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2h9c", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2h9c|  PDB=2h9c  |  SCENE=  }}
-'''Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa'''
+==Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa==
+<StructureSection load='2h9c' size='340' side='right'caption='[[2h9c]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2h9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H9C 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]] 2.35&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=2h9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9c OCA], [https://pdbe.org/2h9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9c RCSB], [https://www.ebi.ac.uk/pdbsum/2h9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9c ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PCHB_PSEAE PCHB_PSEAE] Has isochorismate-pyruvate lyase activity. Probably involved in the conversion of isochorismate to salicylate and pyruvate.
+== 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/h9/2h9c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2h9c ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets.
-==Overview==
+Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa.,Zaitseva J, Lu J, Olechoski KL, Lamb AL J Biol Chem. 2006 Nov 3;281(44):33441-9. Epub 2006 Aug 16. PMID:16914555<ref>PMID:16914555</ref>
-Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-H9C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9C OCA].
+</div>
+<div class="pdbe-citations 2h9c" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa., Zaitseva J, Lu J, Olechoski KL, Lamb AL, J Biol Chem. 2006 Nov 3;281(44):33441-9. Epub 2006 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16914555 16914555]
+*[[Isochorismate pyruvate lyase|Isochorismate pyruvate lyase]]
-[[Category: Pseudomonas aeruginosa]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Lamb, A L.]]
+__TOC__
-[[Category: Lu, J.]]
+</StructureSection>
-[[Category: Zaitseva, J.]]
+[[Category: Large Structures]]
-[[Category: Intertwinded dimer]]
+[[Category: Pseudomonas aeruginosa PAO1]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:01:03 2008''
+[[Category: Lamb AL]]
+[[Category: Lu J]]
+[[Category: Zaitseva J]]