2gu5: Difference between revisions
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[[Image:2gu5.gif|left|200px]] | [[Image:2gu5.gif|left|200px]] | ||
'''E. coli methionine aminopeptidase in complex with NleP, 1: 1, di-metalated''' | {{Structure | ||
|PDB= 2gu5 |SIZE=350|CAPTION= <scene name='initialview01'>2gu5</scene>, resolution 1.600Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=NLP:(1-AMINO-PENTYL)-PHOSPHONIC ACID'>NLP</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 in complex with NleP, 1: 1, di-metalated''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2GU5 is a [ | 2GU5 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=2GU5 OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis of catalysis by monometalated methionine aminopeptidase., Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP, Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9470-5. Epub 2006 Jun 12. PMID:[http:// | Structural basis of catalysis by monometalated methionine aminopeptidase., Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP, Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9470-5. Epub 2006 Jun 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16769889 16769889] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
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[[Category: mononuclear]] | [[Category: mononuclear]] | ||
''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 17:09:09 2008'' | ||
Revision as of 18:09, 20 March 2008
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| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 in complex with NleP, 1: 1, di-metalated
OverviewOverview
Methionine aminopeptidase (MetAP) removes the amino-terminal methionine residue from newly synthesized proteins, and it is a target for the development of antibacterial and anticancer agents. Available x-ray structures of MetAP, as well as other metalloaminopeptidases, show an active site containing two adjacent divalent metal ions bridged by a water molecule or hydroxide ion. The predominance of dimetalated structures leads naturally to proposed mechanisms of catalysis involving both metal ions. However, kinetic studies indicate that in many cases, only a single metal ion is required for full activity. By limiting the amount of metal ion present during crystal growth, we have now obtained a crystal structure for a complex of Escherichia coli MetAP with norleucine phosphonate, a transition-state analog, and only a single Mn(II) ion bound at the active site in the position designated M1, and three related structures of the same complex that show the transition from the mono-Mn(II) form to the di-Mn(II) form. An unliganded structure was also solved. In view of the full kinetic competence of the monometalated MetAP, the much weaker binding constant for occupancy of the M2 site compared with the M1 site, and the newly determined structures, we propose a revised mechanism of peptide bond hydrolysis by E. coli MetAP. We also suggest that the crystallization of dimetalated forms of metallohydrolases may, in some cases, be a misleading experimental artifact, and caution must be taken when structures are generated to aid in elucidation of reaction mechanisms or to support structure-aided drug design efforts.
About this StructureAbout this Structure
2GU5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of catalysis by monometalated methionine aminopeptidase., Ye QZ, Xie SX, Ma ZQ, Huang M, Hanzlik RP, Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9470-5. Epub 2006 Jun 12. PMID:16769889
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