2uzf: Difference between revisions
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<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://www.rcsb.org/pdb/explore.do?structureId=2uzf RCSB], [http://www.ebi.ac.uk/pdbsum/2uzf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/MENB_STAAC MENB_STAAC]] Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) (Probable). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Naphthoate synthase]] | [[Category: Naphthoate synthase]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Buetow, L | [[Category: Buetow, L]] | ||
[[Category: Hunter, W N | [[Category: Hunter, W N]] | ||
[[Category: Ulaganathan, V | [[Category: Ulaganathan, V]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Menaquinone biosynthesis]] | [[Category: Menaquinone biosynthesis]] | ||
Revision as of 16:12, 25 December 2014
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
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 PubMedVitamin 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
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