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1def

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[[Image:1def.gif|left|200px]]
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{{STRUCTURE_1def| PDB=1def | SCENE= }}
{{STRUCTURE_1def| PDB=1def | SCENE= }}
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'''PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES'''
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===PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES===
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==Overview==
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Escherichia coli peptide deformylase, a member of the zinc metalloproteases family, is made up of an active core domain composed of 147 residues and of an additional and dispensable C-terminal tail of 21 residues. The three-dimensional structure of the catalytic core could be studied by NMR. 1H and 15N NMR resonances assignments were obtained by two-dimensional and three-dimensional heteronuclear spectroscopy. The structure could be calculated using a set of 1015 restraints for the 147 residues of the enzyme. The overall structure is composed of a series of antiparallel beta-strands which surround two perpendicular alpha-helices. The C-terminal helix contains the HEXXH motif, which is crucial for activity. This helical arrangement and the way the histidines bind the zinc ion clearly are structurally reminiscent of the other members of the metalloprotease family, such as thermolysin or metzincins. Nevertheless, the overall arrangement of secondary and tertiary structures of peptide deformylase and the positioning of its third zinc ligand (a cysteine) are quite different from those of the other members of the family. These discrepancies, together with several biochemical differences, lead us to propose that peptide deformylase is the first example of a new class of the zinc-metalloproteases family. Studies of the interaction of peptide deformylase with either an inhibitor of the reaction or a product of the catalysed reaction, Met-Ala-Ser, as well as comparisons with the structures of other enzymes of the family, have enabled us to delineate the area corresponding to their binding site. The structural basis of the specificity of recognition of the formyl group is discussed in the context of the protease superfamily.
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(as it appears on PubMed at http://www.pubmed.gov), where 8845003 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8845003}}
==About this Structure==
==About this Structure==
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1DEF 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=1DEF OCA].
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1DEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEF OCA].
==Reference==
==Reference==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Zinc metalloprotease]]
[[Category: Zinc metalloprotease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:45:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:54:06 2008''

Revision as of 19:54, 30 June 2008

Image:1def.png

Template:STRUCTURE 1def

PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES

Template:ABSTRACT PUBMED 8845003

About this Structure

1DEF is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase., Meinnel T, Blanquet S, Dardel F, J Mol Biol. 1996 Sep 27;262(3):375-86. PMID:8845003

Page seeded by OCA on Mon Jun 30 22:54:06 2008

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