1def
From Proteopedia
(New page: 200px<br /> <applet load="1def" size="450" color="white" frame="true" align="right" spinBox="true" caption="1def" /> '''PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1DEF 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 ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEF OCA]]. | + | 1DEF 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 ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEF OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8845003 8845003] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8845003 8845003] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Formylmethionine deformylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dardel, F.]] | [[Category: Dardel, F.]] | ||
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[[Category: zinc metalloprotease]] | [[Category: zinc metalloprotease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:56:54 2007'' |
Revision as of 08:52, 30 October 2007
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PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES
Overview
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 ... [(full description)]
About this Structure
1DEF is a [Single protein] structure of sequence from [Escherichia coli] with ZN as [ligand]. Active as [Formylmethionine deformylase], with EC number [3.5.1.31]. Structure known Active Site: CAT. Full crystallographic 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
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