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| - | [[Image:1i29.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1i29.png|left|200px]] |
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| | {{STRUCTURE_1i29| PDB=1i29 | SCENE= }} | | {{STRUCTURE_1i29| PDB=1i29 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF CSDB COMPLEXED WITH L-PROPARGYLGLYCINE'''
| + | ===CRYSTAL STRUCTURE OF CSDB COMPLEXED WITH L-PROPARGYLGLYCINE=== |
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| - | ==Overview==
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| - | Escherichia coli CsdB is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes both cysteine desulfuration and selenocysteine deselenation. The enzyme has a high specific activity for L-selenocysteine relative to L-cysteine. On the other hand, its paralog, IscS, exhibits higher activity for L-cysteine, which acts as a sulfur donor during the biosynthesis of the iron-sulfur cluster and 4-thiouridine. The structure of CsdB complexed with L-propargylglycine was determined by X-ray crystallography at 2.8 A resolution. The overall polypeptide fold of the complex is similar to that of the uncomplexed enzyme, indicating that no significant structural change occurs upon formation of the complex. In the complex, propargylglycine forms a Schiff base with PLP, providing the features of the external aldimine formed in the active site. The Cys364 residue, which is essential for the activity of CsdB toward L-cysteine but not toward L-selenocysteine, is clearly visible on a loop of the extended lobe (Thr362-Arg375) in all enzyme forms studied, in contrast to the corresponding disordered loop (Ser321-Arg332) of the Thermotoga maritima NifS-like protein, which is closely related to IscS. The extended lobe of CsdB has an 11-residue deletion compared with that of the NifS-like protein. These facts suggest that the restricted flexibility of the Cys364-anchoring extended lobe in CsdB may be responsible for the ability of the enzyme to discriminate between selenium and sulfur.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11983074}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11983074 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11983074}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mihara, H.]] | | [[Category: Mihara, H.]] |
| | [[Category: External aldimine]] | | [[Category: External aldimine]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:29:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:18:19 2008'' |
Revision as of 07:18, 1 July 2008
Template:STRUCTURE 1i29
CRYSTAL STRUCTURE OF CSDB COMPLEXED WITH L-PROPARGYLGLYCINE
Template:ABSTRACT PUBMED 11983074
About this Structure
1I29 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine., Mihara H, Fujii T, Kato S, Kurihara T, Hata Y, Esaki N, J Biochem. 2002 May;131(5):679-85. PMID:11983074
Page seeded by OCA on Tue Jul 1 10:18:19 2008
