2am1

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[[Image:2am1.gif|left|200px]]
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{{STRUCTURE_2am1| PDB=2am1 | SCENE= }}
{{STRUCTURE_2am1| PDB=2am1 | SCENE= }}
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'''sp protein ligand 1'''
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===sp protein ligand 1===
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==Overview==
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In a broad genomics analysis to find novel protein targets for antibiotic discovery, MurF was identified as an essential gene product for Streptococcus pneumonia that catalyzes a critical reaction in the biosynthesis of the peptidoglycan in the formation of the cell wall. Lacking close relatives in mammalian biology, MurF presents attractive characteristics as a potential drug target. Initial screening of the Abbott small-molecule compound collection identified several compounds for further validation as pharmaceutical leads. Here we report the integrated efforts of NMR and X-ray crystallography, which reveal the multidomain structure of a MurF-inhibitor complex in a compact conformation that differs dramatically from related structures. The lead molecule is bound in the substrate-binding region and induces domain closure, suggestive of the domain arrangement for the as yet unobserved transition state conformation for MurF enzymes. The results form a basis for directed optimization of the compound lead by structure-based design to explore the suitability of MurF as a pharmaceutical target.
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(as it appears on PubMed at http://www.pubmed.gov), where 16322581 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16322581}}
==About this Structure==
==About this Structure==
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[[Category: Walter, K A.]]
[[Category: Walter, K A.]]
[[Category: Ligase]]
[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:12:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:35:15 2008''

Revision as of 13:35, 27 July 2008

Template:STRUCTURE 2am1

sp protein ligand 1

Template:ABSTRACT PUBMED 16322581

About this Structure

2AM1 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure., Longenecker KL, Stamper GF, Hajduk PJ, Fry EH, Jakob CG, Harlan JE, Edalji R, Bartley DM, Walter KA, Solomon LR, Holzman TF, Gu YG, Lerner CG, Beutel BA, Stoll VS, Protein Sci. 2005 Dec;14(12):3039-47. PMID:16322581

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