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| [[Image:2am2.gif|left|200px]] | | {{Seed}} |
| | [[Image:2am2.png|left|200px]] |
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| {{STRUCTURE_2am2| PDB=2am2 | SCENE= }} | | {{STRUCTURE_2am2| PDB=2am2 | SCENE= }} |
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| '''sp protein ligand 2'''
| | ===sp protein ligand 2=== |
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16322581}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16322581 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16322581}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Walter, K A.]] | | [[Category: Walter, K A.]] |
| [[Category: Ligase]] | | [[Category: Ligase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:12:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:19:20 2008'' |
