1hnd: Difference between revisions

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-[[Image:1hnd.jpg|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX==
-|PDB= 1hnd |SIZE=350|CAPTION= <scene name='initialview01'>1hnd</scene>, resolution 1.6&Aring;
+<StructureSection load='1hnd' size='340' side='right'caption='[[1hnd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>
+<table><tr><td colspan='2'>[[1hnd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HND FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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]] 1.6&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=1hnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnd OCA], [https://pdbe.org/1hnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnd RCSB], [https://www.ebi.ac.uk/pdbsum/1hnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnd ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1hn9|1hn9]], [[1hnh|1hnh]], [[1hnj|1hnj]], [[1hnk|1hnk]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnd OCA], [http://www.ebi.ac.uk/pdbsum/1hnd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hnd RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
+== 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/hn/1hnd_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=1hnd ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX'''
+==See Also==
+*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing enzyme that plays central roles in fatty acid biosynthesis. Three-dimensional structures of E. coli FabH in the presence and absence of ligands have been refined to 1.46 A resolution. The structures of improved accuracy revealed detailed interactions involved in ligand binding. These structures also provided new insights into the FabH mechanism, e.g. the possible role of a water or hydroxyl anion in Cys112 deprotonation. A structure of the apo enzyme uncovered large conformational changes in the active site, exemplified by the disordering of four essential loops (84-86, 146-152, 185-217 and 305-307) and the movement of catalytic residues (Cys112 and His244). The disordering of the loops leads to greater than 50 % reduction in the FabH dimer interface, suggesting a dynamic nature for an unusually large portion of the dimer interface. The existence of a large solvent-accessible channel in the dimer interface as well as two cis-peptides (cis-Pro88 and cis-Phe308) in two of the disordered loops may explain the observed structural instabilities.
-==About this Structure==
-HND is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HND OCA].
-==Reference==
-Refined structures of beta-ketoacyl-acyl carrier protein synthase III., Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK, J Mol Biol. 2001 Mar 16;307(1):341-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11243824 11243824]
-[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Head, M.]]
+[[Category: Head M]]
-[[Category: Janson, C A.]]
+[[Category: Janson CA]]
-[[Category: Konstantinidis, A K.]]
+[[Category: Konstantinidis AK]]
-[[Category: Lonsdale, J.]]
+[[Category: Lonsdale J]]
-[[Category: Qiu, X.]]
+[[Category: Qiu X]]
-[[Category: Smith, W W.]]
+[[Category: Smith WW]]
-[[Category: fabh]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:59 2008''