2qj3
From Proteopedia
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|PDB= 2qj3 |SIZE=350|CAPTION= <scene name='initialview01'>2qj3</scene>, resolution 3.00Å | |PDB= 2qj3 |SIZE=350|CAPTION= <scene name='initialview01'>2qj3</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </span> |
|GENE= fabD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= fabD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qj3 OCA], [http://www.ebi.ac.uk/pdbsum/2qj3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qj3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ghadbane, H.]] | [[Category: Ghadbane, H.]] | ||
[[Category: Kremer, L.]] | [[Category: Kremer, L.]] | ||
- | [[Category: NI]] | ||
[[Category: fatty acid synthase]] | [[Category: fatty acid synthase]] | ||
[[Category: malonyl-coa]] | [[Category: malonyl-coa]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:49:53 2008'' |
Revision as of 01:49, 31 March 2008
| |||||||
, resolution 3.00Å | |||||||
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Ligands: | |||||||
Gene: | fabD (Mycobacterium tuberculosis) | ||||||
Activity: | [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Mycobacterium tuberculosis FabD
Overview
Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.
About this Structure
2QJ3 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)., Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):831-5. Epub 2007 Sep 19. PMID:17909282[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
Page seeded by OCA on Mon Mar 31 04:49:53 2008