2q94: Difference between revisions
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[[Image:2q94.jpg|left|200px]] | [[Image:2q94.jpg|left|200px]] | ||
'''E. coli methionine aminopeptidase Mn-form with inhibitor A04''' | {{Structure | ||
|PDB= 2q94 |SIZE=350|CAPTION= <scene name='initialview01'>2q94</scene>, resolution 1.630Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=A04:'>A04</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] | |||
|GENE= map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''E. coli methionine aminopeptidase Mn-form with inhibitor A04''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2Q94 is a [ | 2Q94 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q94 OCA]. | ||
==Reference== | ==Reference== | ||
Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes., Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ, BMC Struct Biol. 2007 Dec 19;7:84. PMID:[http:// | Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes., Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ, BMC Struct Biol. 2007 Dec 19;7:84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18093325 18093325] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
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[[Category: mn(ii)-form]] | [[Category: mn(ii)-form]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:23:15 2008'' | ||
Revision as of 19:23, 20 March 2008
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| , resolution 1.630Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | map (Escherichia coli) | ||||||
| Activity: | Methionyl aminopeptidase, with EC number 3.4.11.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E. coli methionine aminopeptidase Mn-form with inhibitor A04
OverviewOverview
BACKGROUND: Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts. RESULTS: Five new X-ray structures of such enzyme-inhibitor complexes were obtained. Analysis of these and other three similar structures reveals the adaptability of a surface-exposed loop bearing Y62, H63, G64 and Y65 (the YHGY loop) that is an integral part of the substrate and inhibitor binding pocket. This adaptability is important for accommodating inhibitors with variations in size. When compared with the human isozymes, this loop either becomes buried in the human type I enzyme due to an N-terminal extension that covers its position or is replaced by a unique insert in the human type II enzyme. CONCLUSION: The adaptability of the YHGY loop in E. coli methionine aminopeptidase, and likely in other bacterial methionine aminopeptidases, enables the enzyme active pocket to accommodate inhibitors of differing size. The differences in this adaptable loop between the bacterial and human methionine aminopeptidases is a structural feature that can be exploited to design inhibitors of bacterial methionine aminopeptidases as therapeutic agents with minimal inhibition of the corresponding human enzymes.
About this StructureAbout this Structure
2Q94 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes., Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ, BMC Struct Biol. 2007 Dec 19;7:84. PMID:18093325
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