1bs4
From Proteopedia
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| - | [[Image:1bs4.gif|left|200px]] | + | [[Image:1bs4.gif|left|200px]] |
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| - | '''PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL''' | + | {{Structure |
| + | |PDB= 1bs4 |SIZE=350|CAPTION= <scene name='initialview01'>1bs4</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=ZNA:One+Peg+Molecule+Is+Located+In+Active+Site+Near+Zn+Ion'>ZNA</scene>, <scene name='pdbsite=ZNB:One+Peg+Molecule+Is+Located+In+Active+Site+Near+Zn+Ion'>ZNB</scene> and <scene name='pdbsite=ZNC:One+Peg+Molecule+Is+Located+In+Active+Site+Near+Zn+Ion'>ZNC</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=2PE:NONAETHYLENE GLYCOL'>2PE</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] | ||
| + | |GENE= DEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BS4 is a [ | + | 1BS4 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=1BS4 OCA]. |
==Reference== | ==Reference== | ||
| - | Iron center, substrate recognition and mechanism of peptide deformylase., Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF, Nat Struct Biol. 1998 Dec;5(12):1053-8. PMID:[http:// | + | Iron center, substrate recognition and mechanism of peptide deformylase., Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF, Nat Struct Biol. 1998 Dec;5(12):1053-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9846875 9846875] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Formylmethionine deformylase]] | [[Category: Formylmethionine deformylase]] | ||
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[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
| - | ''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 10:15:01 2008'' |
Revision as of 08:15, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , and | ||||||
| Gene: | DEF (Escherichia coli) | ||||||
| Activity: | Formylmethionine deformylase, with EC number 3.5.1.31 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL
Overview
Eubacterial proteins are synthesized with a formyl group at the N-terminus which is hydrolytically removed from the nascent chain by the mononuclear iron enzyme peptide deformylase. Catalytic efficiency strongly depends on the identity of the bound metal. We have determined by X-ray crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli enzyme and a structure in complex with the reaction product Met-Ala-Ser. The structure of the complex, with the tripeptide bound at the active site, suggests detailed models for the mechanism of substrate recognition and catalysis. Differences of the protein structures due to the identity of the bound metal are extremely small and account only for the observation that Zn2+ binds more tightly than Fe2+ or Ni2+. The striking loss of catalytic activity of the Zn2+ form could be caused by its reluctance to change between tetrahedral and five-fold metal coordination believed to occur during catalysis. N-terminal formylation and subsequent deformylation
About this Structure
1BS4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Iron center, substrate recognition and mechanism of peptide deformylase., Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF, Nat Struct Biol. 1998 Dec;5(12):1053-8. PMID:9846875
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