1bs6
From Proteopedia
(New page: 200px<br /><applet load="1bs6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bs6, resolution 2.10Å" /> '''PEPTIDE DEFORMYLASE ...) |
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| - | [[Image:1bs6.gif|left|200px]]<br /><applet load="1bs6" size=" | + | [[Image:1bs6.gif|left|200px]]<br /><applet load="1bs6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bs6, resolution 2.10Å" /> | caption="1bs6, resolution 2.10Å" /> | ||
'''PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER'''<br /> | '''PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Eubacterial proteins are synthesized with a formyl group at the N-terminus | + | 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== | ==About this Structure== | ||
| - | 1BS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and NI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1BS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Schultz, S.]] | [[Category: Schultz, S.]] | ||
| - | [[Category: Wagner, A | + | [[Category: Wagner, A F.V.]] |
[[Category: NI]] | [[Category: NI]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: iron metalloprotease; protein synthesis]] | [[Category: iron metalloprotease; protein synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:30 2008'' |
Revision as of 09:58, 21 February 2008
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PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER
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
1BS6 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 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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