1zow
From Proteopedia
(New page: 200px<br /><applet load="1zow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zow, resolution 2.Å" /> '''Crystal Structure of S...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zow.gif|left|200px]]<br /><applet load="1zow" size=" | + | [[Image:1zow.gif|left|200px]]<br /><applet load="1zow" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zow, resolution 2.Å" /> | caption="1zow, resolution 2.Å" /> | ||
'''Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III'''<br /> | '''Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III'''<br /> | ||
==Overview== | ==Overview== | ||
| - | beta-Ketoacyl-ACP synthase III (FabH), an essential enzyme for bacterial | + | beta-Ketoacyl-ACP synthase III (FabH), an essential enzyme for bacterial viability, catalyzes the initiation of fatty acid elongation by condensing malonyl-ACP with acetyl-CoA. We have determined the crystal structure of FabH from Staphylococcus aureus, a Gram-positive human pathogen, to 2 A resolution. Although the overall structure of S. aureus FabH is similar to that of Escherichia coli FabH, the primer binding pocket in S. aureus FabH is significantly larger than that present in E. coli FabH. The structural differences, which agree with kinetic parameters, provide explanation for the observed varying substrate specificity for E. coli and S. aureus FabH. The rank order of activity of S. aureus FabH with various acyl-CoA primers was as follows: isobutyryl- > hexanoyl- > butyryl- > isovaleryl- >> acetyl-CoA. The availability of crystal structure may aid in designing potent, selective inhibitors of S. aureus FabH. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZOW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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:// | + | 1ZOW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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=1ZOW OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Choudhry, A | + | [[Category: Choudhry, A E.]] |
| - | [[Category: Daines, R | + | [[Category: Daines, R A.]] |
[[Category: Grooms, M.]] | [[Category: Grooms, M.]] | ||
| - | [[Category: Janson, C | + | [[Category: Janson, C A.]] |
| - | [[Category: Khandekar, S | + | [[Category: Khandekar, S S.]] |
| - | [[Category: Lonsdale, J | + | [[Category: Lonsdale, J T.]] |
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
[[Category: fabh]] | [[Category: fabh]] | ||
[[Category: fatty acid biosynthesis]] | [[Category: fatty acid biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:41 2008'' |
Revision as of 14:17, 21 February 2008
|
Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III
Overview
beta-Ketoacyl-ACP synthase III (FabH), an essential enzyme for bacterial viability, catalyzes the initiation of fatty acid elongation by condensing malonyl-ACP with acetyl-CoA. We have determined the crystal structure of FabH from Staphylococcus aureus, a Gram-positive human pathogen, to 2 A resolution. Although the overall structure of S. aureus FabH is similar to that of Escherichia coli FabH, the primer binding pocket in S. aureus FabH is significantly larger than that present in E. coli FabH. The structural differences, which agree with kinetic parameters, provide explanation for the observed varying substrate specificity for E. coli and S. aureus FabH. The rank order of activity of S. aureus FabH with various acyl-CoA primers was as follows: isobutyryl- > hexanoyl- > butyryl- > isovaleryl- >> acetyl-CoA. The availability of crystal structure may aid in designing potent, selective inhibitors of S. aureus FabH.
About this Structure
1ZOW is a Single protein structure of sequence from Staphylococcus aureus. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus., Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT, Khandekar SS, Protein Sci. 2005 Aug;14(8):2087-94. Epub 2005 Jun 29. PMID:15987898
Page seeded by OCA on Thu Feb 21 16:17:41 2008
