1bsk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bsk]] is a 1 chain structure with 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=1BSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BSK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1bsk]] is a 1 chain structure with 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=1BSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BSK FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLN:(S)-2-(PHOSPHONOXY)CAPROYL-L-LEUCYL-P-NITROANILIDE'>MLN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLN:(S)-2-(PHOSPHONOXY)CAPROYL-L-LEUCYL-P-NITROANILIDE'>MLN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-formylmethionylaminoacyl-tRNA_deformylase N-formylmethionylaminoacyl-tRNA deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.27 3.5.1.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-formylmethionylaminoacyl-tRNA_deformylase N-formylmethionylaminoacyl-tRNA deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.27 3.5.1.27] </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=1bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bsk RCSB], [http://www.ebi.ac.uk/pdbsum/1bsk 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=1bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bsk RCSB], [http://www.ebi.ac.uk/pdbsum/1bsk PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: N-formylmethionylaminoacyl-tRNA deformylase]] | [[Category: N-formylmethionylaminoacyl-tRNA deformylase]] | ||
[[Category: Chan, M K | [[Category: Chan, M K]] | ||
[[Category: Gong, W | [[Category: Gong, W]] | ||
[[Category: Hao, B | [[Category: Hao, B]] | ||
[[Category: Hu, Y | [[Category: Hu, Y]] | ||
[[Category: Pei, D | [[Category: Pei, D]] | ||
[[Category: Rajagopalan, P T | [[Category: Rajagopalan, P T]] | ||
[[Category: Deformylase]] | [[Category: Deformylase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
[[Category: Metalloproteinase]] | [[Category: Metalloproteinase]] | ||
Revision as of 13:36, 22 December 2014
ZINC DEFORMYLASE INHIBITOR COMPLEX FROM E.COLIZINC DEFORMYLASE INHIBITOR COMPLEX FROM E.COLI
Structural highlights
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 PubMedWhile protein synthesis in bacteria begins with a formylated methionine, the formyl group of the nascent polypeptide is removed by peptide deformylase. Since eukaryotic protein synthesis does not involve formylation and deformylation at the N-terminus, there has been increasing interest in peptide deformylase as a potential target for antibacterial chemotherapy. Toward this end and to aid in the design of effective antibiotics targeting peptide deformylase, the structures of the protein-inhibitor complexes of both the cobalt and the zinc containing Escherichia coli peptide deformylase bound to the transition-state analogue, (S)-2-O-(H-phosphonoxy)-L-caproyl-L-leucyl-p-nitroanilide (PCLNA), have been determined. The proteins for both deformylase-inhibitor complexes show basically the same fold as for the native enzyme. The PCLNA inhibitor adopts an extended conformation and fits nicely into a hydrophobic cavity located near the metal site. On the basis of these structures, guidelines for the design of high-affinity deformylase inhibitors are suggested. As our results show that the protein residues which interact with the PCLNA inhibitor are conserved over a wide variety of species, we suggest that antibiotics targeting deformylase could have wide applicability. Structural basis for the design of antibiotics targeting peptide deformylase.,Hao B, Gong W, Rajagopalan PT, Zhou Y, Pei D, Chan MK Biochemistry. 1999 Apr 13;38(15):4712-9. PMID:10200158[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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