1bs4
From Proteopedia
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| - | [[Image:1bs4.gif|left|200px]]<br /> | + | [[Image:1bs4.gif|left|200px]]<br /><applet load="1bs4" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bs4" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1bs4, resolution 1.90Å" /> | caption="1bs4, resolution 1.90Å" /> | ||
'''PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL'''<br /> | '''PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BS4 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, ZN and 2PE 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] | + | 1BS4 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, ZN and 2PE 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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BS4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:32:50 2007'' |
Revision as of 12:23, 18 December 2007
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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 with SO4, ZN and 2PE as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Known structural/functional Sites: , and . 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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