1bsj
From Proteopedia
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|PDB= 1bsj |SIZE=350|CAPTION= <scene name='initialview01'>1bsj</scene>, resolution 3.0Å | |PDB= 1bsj |SIZE=350|CAPTION= <scene name='initialview01'>1bsj</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MLN:(S)-2-(PHOSPHONOXY)CAPROYL-L-LEUCYL-P-NITROANILIDE'>MLN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsj OCA], [http://www.ebi.ac.uk/pdbsum/1bsj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bsj RCSB]</span> | ||
}} | }} | ||
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[[Category: Pei, D.]] | [[Category: Pei, D.]] | ||
[[Category: Rajagopalan, P T.]] | [[Category: Rajagopalan, P T.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: MLN]] | ||
| - | [[Category: PO4]] | ||
[[Category: deformylase]] | [[Category: deformylase]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
[[Category: metalloproteinase]] | [[Category: metalloproteinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:07:24 2008'' |
Revision as of 16:07, 30 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | N-formylmethionylaminoacyl-tRNA deformylase, with EC number 3.5.1.27 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COBALT DEFORMYLASE INHIBITOR COMPLEX FROM E.COLI
Overview
While 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.
About this Structure
1BSJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 19:07:24 2008
