1hnk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:13, 9 August 2023) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hnk.jpg|left|200px]]<br /><applet load="1hnk" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1hnk, resolution 1.9&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM==
-
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='1hnk' size='340' side='right'caption='[[1hnk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
</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/1hnk_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=1hnk ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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==
+
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>
-
1HNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNK OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
+
<div class="pdbe-citations 1hnk" style="background-color:#fffaf0;"></div>
-
[[Category: Escherichia coli]]
+
-
[[Category: Single protein]]
+
-
[[Category: Head, M.]]
+
-
[[Category: Janson, C.A.]]
+
-
[[Category: Konstantinidis, A.K.]]
+
-
[[Category: Lonsdale, J.]]
+
-
[[Category: Qiu, X.]]
+
-
[[Category: Smith, W.W.]]
+
-
[[Category: fabh]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:21 2008''
+
==See Also==
 +
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Escherichia coli]]
 +
[[Category: Large Structures]]
 +
[[Category: Head M]]
 +
[[Category: Janson CA]]
 +
[[Category: Konstantinidis AK]]
 +
[[Category: Lonsdale J]]
 +
[[Category: Qiu X]]
 +
[[Category: Smith WW]]

Current revision

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

PDB ID 1hnk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hnk"
Personal tools