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2ier

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[[Image:2ier.gif|left|200px]]
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{{STRUCTURE_2ier| PDB=2ier | SCENE= }}
{{STRUCTURE_2ier| PDB=2ier | SCENE= }}
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'''Crystal Structure of Aquifex aeolicus LpxC Complexed with Uridine 5'-Diphosphate'''
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===Crystal Structure of Aquifex aeolicus LpxC Complexed with Uridine 5'-Diphosphate===
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==Overview==
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LpxC is a zinc metalloenzyme that catalyzes the first committed step in the biosynthesis of lipid A, a vital component of the outer membrane of Gram-negative bacteria. Accordingly, the inhibition of LpxC is an attractive strategy for the treatment of Gram-negative bacterial infections. Here, we report the 2.7 A resolution X-ray crystal structure of LpxC from Aquifex aeolicus complexed with uridine 5'-diphosphate (UDP), and the 3.1 A resolution structure of LpxC complexed with pyrophosphate. The X-ray crystal structure of the LpxC-UDP complex provides the first view of interactions likely to be exploited by the substrate UDP group in the "basic patch" of the active site. The diphosphate group of UDP makes hydrogen bond interactions with strictly conserved residue K239 as well as solvent molecules. The ribose moiety of UDP interacts with partially conserved residue E197. The UDP uracil group hydrogen bonds with both the backbone NH group and the backbone carbonyl group of E160, and with the backbone NH group of K162 through an intervening water molecule. Finally, the alpha-phosphate and uracil groups of UDP interact with R143 and R262 through intervening water molecules. The structure of LpxC complexed with pyrophosphate reveals generally similar intermolecular interactions in the basic patch. Unexpectedly, diphosphate binding in both complexes is accompanied by coordination to an additional zinc ion, resulting in the identification of a new metal-binding site termed the E-site. The structures of the LpxC-UDP and LpxC-pyrophosphate complexes provide new insights with regard to substrate recognition in the basic patch and metal ion coordination in the active site of LpxC.
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(as it appears on PubMed at http://www.pubmed.gov), where 17176043 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17176043}}
==About this Structure==
==About this Structure==
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[[Category: Gennadios, H A.]]
[[Category: Gennadios, H A.]]
[[Category: Alpha + beta fold]]
[[Category: Alpha + beta fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:25:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:22:42 2008''

Revision as of 18:22, 27 July 2008

Image:2ier.png

Template:STRUCTURE 2ier

Crystal Structure of Aquifex aeolicus LpxC Complexed with Uridine 5'-Diphosphate

Template:ABSTRACT PUBMED 17176043

About this Structure

2IER is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Binding of uridine 5'-diphosphate in the "basic patch" of the zinc deacetylase LpxC and implications for substrate binding., Gennadios HA, Christianson DW, Biochemistry. 2006 Dec 26;45(51):15216-23. Epub 2006 Nov 30. PMID:17176043

Page seeded by OCA on Sun Jul 27 21:22:42 2008

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