1hnd: Difference between revisions

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New page: left|200px<br /><applet load="1hnd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hnd, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1hnd.jpg|left|200px]]<br /><applet load="1hnd" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX==
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.
<StructureSection load='1hnd' size='340' side='right'caption='[[1hnd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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>


==About this Structure==
==See Also==
1HND is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with COA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HND OCA].
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11243824 11243824]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Escherichia coli]]
[[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: COA]]
[[Category: fabh]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:40:16 2007''

Latest revision as of 10:28, 7 February 2024

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEXCRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX

Structural highlights

1hnd is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1hnd, resolution 1.60Å

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