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1hnk

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[[Image:1hnk.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM==
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|PDB= 1hnk |SIZE=350|CAPTION= <scene name='initialview01'>1hnk</scene>, resolution 1.9&Aring;
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<StructureSection load='1hnk' size='340' side='right'caption='[[1hnk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1hnk]] 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=1HNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNK FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnk OCA], [https://pdbe.org/1hnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnk RCSB], [https://www.ebi.ac.uk/pdbsum/1hnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnk ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1hn9|1hn9]], [[1hnd|1hnd]], [[1hnh|1hnh]], [[1hnj|1hnj]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnk OCA], [http://www.ebi.ac.uk/pdbsum/1hnk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hnk RCSB]</span>
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[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]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hnk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1hnk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM'''
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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:11243824<ref>PMID:11243824</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hnk" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1HNK 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=1HNK OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Head, M.]]
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[[Category: Head M]]
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[[Category: Janson, C A.]]
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[[Category: Janson CA]]
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[[Category: Konstantinidis, A K.]]
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[[Category: Konstantinidis AK]]
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[[Category: Lonsdale, J.]]
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[[Category: Lonsdale J]]
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[[Category: Qiu, X.]]
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[[Category: Qiu X]]
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[[Category: Smith, W W.]]
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[[Category: Smith WW]]
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[[Category: fabh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:06 2008''
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Current revision

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM

PDB ID 1hnk

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