1oxh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1oxh.jpg|left|200px]] | [[Image:1oxh.jpg|left|200px]] | ||
'''The crystal structure of beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus Pneumoniae, Triclinic form''' | {{Structure | ||
|PDB= 1oxh |SIZE=350|CAPTION= <scene name='initialview01'>1oxh</scene>, resolution 2.09Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''The crystal structure of beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus Pneumoniae, Triclinic form''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1OXH is a [ | 1OXH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXH OCA]. | ||
==Reference== | ==Reference== | ||
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae., Price AC, Rock CO, White SW, J Bacteriol. 2003 Jul;185(14):4136-43. PMID:[http:// | The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae., Price AC, Rock CO, White SW, J Bacteriol. 2003 Jul;185(14):4136-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837788 12837788] | ||
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:16:57 2008'' | ||
Revision as of 14:16, 20 March 2008
| |||||||
| , resolution 2.09Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus Pneumoniae, Triclinic form
OverviewOverview
The beta-ketoacyl-acyl carrier protein synthases are members of the thiolase superfamily and are key regulators of bacterial fatty acid synthesis. As essential components of the bacterial lipid metabolic pathway, they are an attractive target for antibacterial drug discovery. We have determined the 1.3 A resolution crystal structure of the beta-ketoacyl-acyl carrier protein synthase II (FabF) from the pathogenic organism Streptococcus pneumoniae. The protein adopts a duplicated betaalphabetaalphabetaalphabetabeta fold, which is characteristic of the thiolase superfamily. The two-fold pseudosymmetry is broken by the presence of distinct insertions in the two halves of the protein. These insertions have evolved to bind the specific substrates of this particular member of the thiolase superfamily. Docking of the pantetheine moiety of the substrate identifies the loop regions involved in substrate binding and indicates roles for specific, conserved residues in the substrate binding tunnel. The active site triad of this superfamily is present in spFabF as His 303, His 337, and Cys 164. Near the active site is an ion pair, Glu 346 and Lys 332, that is conserved in the condensing enzymes but is unusual in our structure in being stabilized by an Mg(2+) ion which interacts with Glu 346. The active site histidines interact asymmetrically with Lys 332, whose positive charge is closer to His 303, and we propose a specific role for the lysine in polarizing the imidazole ring of this histidine. This asymmetry suggests that the two histidines have unequal roles in catalysis and provides new insights into the catalytic mechanisms of these enzymes.
About this StructureAbout this Structure
1OXH is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
ReferenceReference
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae., Price AC, Rock CO, White SW, J Bacteriol. 2003 Jul;185(14):4136-43. PMID:12837788
Page seeded by OCA on Thu Mar 20 13:16:57 2008