2h9c
From Proteopedia
(New page: 200px<br /><applet load="2h9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h9c, resolution 2.350Å" /> '''Native Crystal Stru...) |
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| - | [[Image:2h9c.gif|left|200px]]<br /><applet load="2h9c" size=" | + | [[Image:2h9c.gif|left|200px]]<br /><applet load="2h9c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2h9c, resolution 2.350Å" /> | caption="2h9c, resolution 2.350Å" /> | ||
'''Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa'''<br /> | '''Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A | + | Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets. |
==About this Structure== | ==About this Structure== | ||
| - | 2H9C 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 NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2H9C 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=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lamb, A | + | [[Category: Lamb, A L.]] |
[[Category: Lu, J.]] | [[Category: Lu, J.]] | ||
[[Category: Zaitseva, J.]] | [[Category: Zaitseva, J.]] | ||
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[[Category: intertwinded dimer]] | [[Category: intertwinded dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:30 2008'' |
Revision as of 15:39, 21 February 2008
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Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa
Overview
Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets.
About this Structure
2H9C is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Full crystallographic information is available from OCA.
Reference
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa., Zaitseva J, Lu J, Olechoski KL, Lamb AL, J Biol Chem. 2006 Nov 3;281(44):33441-9. Epub 2006 Aug 16. PMID:16914555
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