1qxw: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qxw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QXW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qxw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QXW FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=M1C:(3S)-3-AMINO-1-(CYCLOPROPYLAMINO)HEPTANE-2,2-DIOL'>M1C</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=M1C:(3S)-3-AMINO-1-(CYCLOPROPYLAMINO)HEPTANE-2,2-DIOL'>M1C</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qxy|1qxy]], [[1qxz|1qxz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qxy|1qxy]], [[1qxz|1qxz]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qxw RCSB], [http://www.ebi.ac.uk/pdbsum/1qxw PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qxw RCSB], [http://www.ebi.ac.uk/pdbsum/1qxw PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/AMPM_STAA1 AMPM_STAA1]] Removes the N-terminal methionine from nascent proteins (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Arcy, A D | [[Category: Arcy, A D]] | ||
[[Category: Dale, G E | [[Category: Dale, G E]] | ||
[[Category: Douangamath, A | [[Category: Douangamath, A]] | ||
[[Category: Oefner, C | [[Category: Oefner, C]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Pita bread fold]] | [[Category: Pita bread fold]] | ||
Revision as of 17:14, 25 December 2014
Crystal structure of Staphyloccocus aureus in complex with an aminoketone inhibitor 54135.Crystal structure of Staphyloccocus aureus in complex with an aminoketone inhibitor 54135.
Structural highlights
Function[AMPM_STAA1] Removes the N-terminal methionine from nascent proteins (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHigh-resolution crystal structures of Staphylococcus aureus methionine aminopeptidase I in complex with various keto heterocycles and aminoketones were determined, and the intermolecular ligand interactions with the enzyme are reported. The compounds are effective inhibitors of the S. aureus enzyme because of the formation of an uncleavable tetrahedral intermediate upon binding. The electron densities unequivocally show the enzyme-catalyzed transition-state analogue mimicking that for amide bond hydrolysis of substrates. Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate.,Douangamath A, Dale GE, D'Arcy A, Almstetter M, Eckl R, Frutos-Hoener A, Henkel B, Illgen K, Nerdinger S, Schulz H, Mac Sweeney A, Thormann M, Treml A, Pierau S, Wadman S, Oefner C J Med Chem. 2004 Mar 11;47(6):1325-8. PMID:14998322[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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