1cs1
From Proteopedia
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| - | [[Image:1cs1.gif|left|200px]] | + | [[Image:1cs1.gif|left|200px]] |
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| - | '''CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1cs1 |SIZE=350|CAPTION= <scene name='initialview01'>1cs1</scene>, resolution 1.5Å | ||
| + | |SITE= <scene name='pdbsite=PLA:Cofactor+Site+Chain+A'>PLA</scene>, <scene name='pdbsite=PLB:Cofactor+Site+Chain+B'>PLB</scene>, <scene name='pdbsite=PLC:Cofactor+Site+Chain+C'>PLC</scene> and <scene name='pdbsite=PLD:Cofactor+Site+Chain+D'>PLD</scene> | ||
| + | |LIGAND= <scene name='pdbligand=DHD:2,4-DIOXO-PENTANEDIOIC ACID'>DHD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.5.1.48 Transferred entry: 2.5.1.48], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.9 4.2.99.9] | ||
| + | |GENE= METB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CS1 is a [ | + | 1CS1 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=1CS1 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution., Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A, EMBO J. 1998 Dec 1;17(23):6827-38. PMID:[http:// | + | Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution., Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A, EMBO J. 1998 Dec 1;17(23):6827-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9843488 9843488] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: DHD]] | [[Category: DHD]] | ||
| - | [[Category: llp-dependent | + | [[Category: llp-dependent enzyme]] |
[[Category: lyase]] | [[Category: lyase]] | ||
[[Category: methionine biosynthesis]] | [[Category: methionine biosynthesis]] | ||
| - | ''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 10:28:10 2008'' |
Revision as of 08:28, 20 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Gene: | METB (Escherichia coli) | ||||||
| Activity: | Transferred entry: 2.5.1.48, with EC number 4.2.99.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI
Overview
The transsulfuration enzyme cystathionine gamma-synthase (CGS) catalyses the pyridoxal 5'-phosphate (PLP)-dependent gamma-replacement of O-succinyl-L-homoserine and L-cysteine, yielding L-cystathionine. The crystal structure of the Escherichia coli enzyme has been solved by molecular replacement with the known structure of cystathionine beta-lyase (CBL), and refined at 1.5 A resolution to a crystallographic R-factor of 20.0%. The enzyme crystallizes as an alpha4 tetramer with the subunits related by non-crystallographic 222 symmetry. The spatial fold of the subunits, with three functionally distinct domains and their quaternary arrangement, is similar to that of CBL. Previously proposed reaction mechanisms for CGS can be checked against the structural model, allowing interpretation of the catalytic and substrate-binding functions of individual active site residues. Enzyme-substrate models pinpoint specific residues responsible for the substrate specificity, in agreement with structural comparisons with CBL. Both steric and electrostatic designs of the active site seem to achieve proper substrate selection and productive orientation. Amino acid sequence and structural alignments of CGS and CBL suggest that differences in the substrate-binding characteristics are responsible for the different reaction chemistries. Because CGS catalyses the only known PLP-dependent replacement reaction at Cgamma of certain amino acids, the results will help in our understanding of the chemical versatility of PLP.
About this Structure
1CS1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution., Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A, EMBO J. 1998 Dec 1;17(23):6827-38. PMID:9843488
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