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==Crystal structure of Staphylococcus aureus 1,4-dihydroxy-2-naphthoyl CoA synthase (MenB) in complex with acetoacetyl CoA==
==Crystal structure of Staphylococcus aureus 1,4-dihydroxy-2-naphthoyl CoA synthase (MenB) in complex with acetoacetyl CoA==
<StructureSection load='2uzf' size='340' side='right' caption='[[2uzf]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2uzf' size='340' side='right' caption='[[2uzf]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2uzf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UZF FirstGlance]. <br>
<table><tr><td colspan='2'>[[2uzf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UZF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Naphthoate_synthase Naphthoate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.36 4.1.3.36] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,4-dihydroxy-2-naphthoyl-CoA_synthase 1,4-dihydroxy-2-naphthoyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.36 4.1.3.36] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uzf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2uzf RCSB], [http://www.ebi.ac.uk/pdbsum/2uzf PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uzf OCA], [http://pdbe.org/2uzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uzf RCSB], [http://www.ebi.ac.uk/pdbsum/2uzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uzf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2uzf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2uzf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Naphthoate synthase]]
[[Category: 1,4-dihydroxy-2-naphthoyl-CoA synthase]]
[[Category: Staphylococcus aureus]]
[[Category: Buetow, L]]
[[Category: Buetow, L]]
[[Category: Hunter, W N]]
[[Category: Hunter, W N]]

Revision as of 00:15, 5 August 2016

Crystal structure of Staphylococcus aureus 1,4-dihydroxy-2-naphthoyl CoA synthase (MenB) in complex with acetoacetyl CoACrystal structure of Staphylococcus aureus 1,4-dihydroxy-2-naphthoyl CoA synthase (MenB) in complex with acetoacetyl CoA

Structural highlights

2uzf is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:1,4-dihydroxy-2-naphthoyl-CoA synthase, with EC number 4.1.3.36
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MENB_STAAC] Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) (Probable).

Evolutionary Conservation

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

Publication Abstract from PubMed

Vitamin K(2), or menaquinone, is an essential cofactor for many organisms and the enzymes involved in its biosynthesis are potential antimicrobial drug targets. One of these enzymes, 1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) from the pathogen Staphylococcus aureus, has been obtained in recombinant form and its quaternary structure has been analyzed in solution. Cubic crystals of the enzyme allowed a low-resolution structure (2.9 A) to be determined. The asymmetric unit consists of two subunits and a crystallographic threefold axis of symmetry generates a hexamer consistent with size-exclusion chromatography. Analytical ultracentrifugation indicates the presence of six states in solution, monomeric through to hexameric, with the dimer noted as being particularly stable. MenB displays the crotonase-family fold with distinct N- and C-terminal domains and a flexible segment of structure around the active site. The smaller C-terminal domain plays an important role in oligomerization and also in substrate binding. The presence of acetoacetyl-CoA in one of the two active sites present in the asymmetric unit indicates how part of the substrate binds and facilitates comparisons with the structure of Mycobacterium tuberculosis MenB.

Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA.,Ulaganathan V, Agacan MF, Buetow L, Tulloch LB, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):908-13., Epub 2007 Oct 20. PMID:18007038[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Ulaganathan V, Agacan MF, Buetow L, Tulloch LB, Hunter WN. Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):908-13., Epub 2007 Oct 20. PMID:18007038 doi:10.1107/S1744309107047720

2uzf, resolution 2.90Å

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