1lqo
From Proteopedia
(New page: 200px<br /><applet load="1lqo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lqo, resolution 2.00Å" /> '''Crystal Strutcure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lqo.gif|left|200px]]<br /><applet load="1lqo" size=" | + | [[Image:1lqo.gif|left|200px]]<br /><applet load="1lqo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lqo, resolution 2.00Å" /> | caption="1lqo, resolution 2.00Å" /> | ||
'''Crystal Strutcure of the Fosfomycin Resistance Protein A (FosA) Containing Bound Thallium Cations'''<br /> | '''Crystal Strutcure of the Fosfomycin Resistance Protein A (FosA) Containing Bound Thallium Cations'''<br /> | ||
| + | |||
| + | ==Overview== | ||
| + | The fosfomycin resistance protein (FosA) catalyzes the Mn(II)- and K+-dependent addition of glutathione to the oxirane of the antibiotic fosfomycin. The crystal structure of FosA from Pseudomonas aeruginosa was solved at a resolution of 1.19 A by multiwavelength anomalous diffraction at the L-III edge of a Tl+ derivative. The structure solution took advantage of the ability of Tl+ to substitute for K+. The existence of multiple Tl sites in the asymmetric unit suggests that this may be a generally useful technique for phasing protein crystal structures. A 1.35 A resolution structure with phosphate bound in the active site shows that the Mn(II) center has a rare four-coordinate geometry. The structure of the fosfomycin complex at 1.19 A resolution indicates that the Mn(II) center is close to five-coordinate with trigonal bipyramidal geometry and a ligand set consisting of two histidines (H7 and H64) and one phosphonate oxygen occupying the equatorial sites and the carboxylate of E110 at one of the apical sites. The oxirane oxygen of the substrate is located at the other apical site but is 0.2 A beyond the average Mn-O distance for five-coordinate Mn(II). The Mn(II) center is proposed to stabilize the alkoxide in the transition state, while the nearby hydroxyl group of T9 acts as a proton donor in the reaction. The K+ ion located 6.5 A from the Mn(II) appears to help orient the substrate for nucleophilic attack. | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with PO4, MN and TL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http:// | + | 1LQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=TL:'>TL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQO OCA]. |
==Reference== | ==Reference== | ||
| Line 11: | Line 14: | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Armstrong, R | + | [[Category: Armstrong, R N.]] |
| - | [[Category: Newcomer, M | + | [[Category: Newcomer, M E.]] |
| - | [[Category: Pharris, R | + | [[Category: Pharris, R E.]] |
| - | [[Category: Rife, C | + | [[Category: Rife, C L.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
| Line 21: | Line 24: | ||
[[Category: thallium binding loop]] | [[Category: thallium binding loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:28 2008'' |
Revision as of 11:47, 21 February 2008
|
Crystal Strutcure of the Fosfomycin Resistance Protein A (FosA) Containing Bound Thallium Cations
Overview
The fosfomycin resistance protein (FosA) catalyzes the Mn(II)- and K+-dependent addition of glutathione to the oxirane of the antibiotic fosfomycin. The crystal structure of FosA from Pseudomonas aeruginosa was solved at a resolution of 1.19 A by multiwavelength anomalous diffraction at the L-III edge of a Tl+ derivative. The structure solution took advantage of the ability of Tl+ to substitute for K+. The existence of multiple Tl sites in the asymmetric unit suggests that this may be a generally useful technique for phasing protein crystal structures. A 1.35 A resolution structure with phosphate bound in the active site shows that the Mn(II) center has a rare four-coordinate geometry. The structure of the fosfomycin complex at 1.19 A resolution indicates that the Mn(II) center is close to five-coordinate with trigonal bipyramidal geometry and a ligand set consisting of two histidines (H7 and H64) and one phosphonate oxygen occupying the equatorial sites and the carboxylate of E110 at one of the apical sites. The oxirane oxygen of the substrate is located at the other apical site but is 0.2 A beyond the average Mn-O distance for five-coordinate Mn(II). The Mn(II) center is proposed to stabilize the alkoxide in the transition state, while the nearby hydroxyl group of T9 acts as a proton donor in the reaction. The K+ ion located 6.5 A from the Mn(II) appears to help orient the substrate for nucleophilic attack.
About this Structure
1LQO is a Single protein structure of sequence from Pseudomonas aeruginosa with , and as ligands. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+)., Rife CL, Pharris RE, Newcomer ME, Armstrong RN, J Am Chem Soc. 2002 Sep 18;124(37):11001-3. PMID:12224946
Page seeded by OCA on Thu Feb 21 13:47:28 2008
