1c0n
From Proteopedia
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| - | [[Image:1c0n.gif|left|200px]] | + | [[Image:1c0n.gif|left|200px]] |
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| - | '''CSDB PROTEIN, NIFS HOMOLOGUE''' | + | {{Structure |
| + | |PDB= 1c0n |SIZE=350|CAPTION= <scene name='initialview01'>1c0n</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CSDB PROTEIN, NIFS HOMOLOGUE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C0N is a [ | + | 1C0N 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=1C0N OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase., Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y, Biochemistry. 2000 Feb 15;39(6):1263-73. PMID:[http:// | + | Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase., Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y, Biochemistry. 2000 Feb 15;39(6):1263-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10684605 10684605] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta fold]] | [[Category: alpha/beta fold]] | ||
| - | ''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 10:18:18 2008'' |
Revision as of 08:18, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CSDB PROTEIN, NIFS HOMOLOGUE
Overview
Escherichia coli CsdB, a NifS homologue with a high specificity for L-selenocysteine, is a pyridoxal 5'-phosphate (PLP)-dependent dimeric enzyme that belongs to aminotransferases class V in fold-type I of PLP enzymes and catalyzes the decomposition of L-selenocysteine into selenium and L-alanine. The crystal structure of the enzyme has been determined by the X-ray crystallographic method of multiple isomorphous replacement and refined to an R-factor of 18.7% at 2.8 A resolution. The subunit structure consists of three parts: a large domain of an alpha/beta-fold containing a seven-stranded beta-sheet flanked by seven helices, a small domain containing a four-stranded antiparallel beta-sheet flanked by three alpha-helices, and an N-terminal segment containing two alpha-helices. The overall fold of the subunit is similar to those of the enzymes belonging to the fold-type I family represented by aspartate aminotransferase. However, CsdB has several structural features that are not observed in other families of the enzymes. A remarkable feature is that an alpha-helix in the lobe extending from the small domain to the large domain in one subunit of the dimer interacts with a beta-hairpin loop protruding from the large domain of the other subunit. The extended lobe and the protruded beta-hairpin loop form one side of a limb of each active site in the enzyme. The most striking structural feature of CsdB lies in the location of a putative catalytic residue; the side chain of Cys364 on the extended lobe of one subunit is close enough to interact with the gamma-atom of a modeled substrate in the active site of the subunit. Moreover, His55 from the other subunit is positioned so that it interacts with the gamma- or beta-atom of the substrate and may be involved in the catalytic reaction. This is the first report on three-dimensional structures of NifS homologues.
About this Structure
1C0N is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase., Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y, Biochemistry. 2000 Feb 15;39(6):1263-73. PMID:10684605
Page seeded by OCA on Thu Mar 20 10:18:18 2008
Categories: Escherichia coli | Single protein | Esaki, N. | Fujii, T. | Hata, Y. | Kurihara, T. | Maeda, M. | Mihara, H. | ACY | PLP | Alpha/beta fold
