1xrb
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1xrb.jpg|left|200px]] | + | [[Image:1xrb.jpg|left|200px]] |
| - | + | ||
| - | '''S-ADENOSYLMETHIONINE SYNTHETASE (MAT, ATP: L-METHIONINE S-ADENOSYLTRANSFERASE, E.C.2.5.1.6) IN WHICH MET RESIDUES ARE REPLACED WITH SELENOMETHIONINE RESIDUES (MSE)''' | + | {{Structure |
| + | |PDB= 1xrb |SIZE=350|CAPTION= <scene name='initialview01'>1xrb</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''S-ADENOSYLMETHIONINE SYNTHETASE (MAT, ATP: L-METHIONINE S-ADENOSYLTRANSFERASE, E.C.2.5.1.6) IN WHICH MET RESIDUES ARE REPLACED WITH SELENOMETHIONINE RESIDUES (MSE)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1XRB is a [ | + | 1XRB 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=1XRB OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of S-adenosylmethionine synthetase., Takusagawa F, Kamitori S, Misaki S, Markham GD, J Biol Chem. 1996 Jan 5;271(1):136-47. PMID:[http:// | + | Crystal structure of S-adenosylmethionine synthetase., Takusagawa F, Kamitori S, Misaki S, Markham GD, J Biol Chem. 1996 Jan 5;271(1):136-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8550549 8550549] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Methionine adenosyltransferase]] | [[Category: Methionine adenosyltransferase]] | ||
| Line 23: | Line 32: | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
| - | ''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 15:13:39 2008'' |
Revision as of 13:13, 20 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Methionine adenosyltransferase, with EC number 2.5.1.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S-ADENOSYLMETHIONINE SYNTHETASE (MAT, ATP: L-METHIONINE S-ADENOSYLTRANSFERASE, E.C.2.5.1.6) IN WHICH MET RESIDUES ARE REPLACED WITH SELENOMETHIONINE RESIDUES (MSE)
Overview
The structure of S-adenosylmethionine synthetase (MAT, ATP:L-methionine S-adenosyltransferase, EC 2.5.1.6.) from Escherichia coli has been determined at 3.0 A resolution by multiple isomorphous replacement using a uranium derivative and the selenomethionine form of the enzyme (SeMAT). The SeMAT data (9 selenomethionine residues out of 383 amino acid residues) have been found to have a sufficient phasing power to determine the structure of the 42,000 molecular weight protein by combining them with the other heavy atom derivative data (multiple isomorphous replacement). The enzyme consists of four identical subunits; two subunits form a spherical tight dimer, and pairs of these dimers form a peanut-shaped tetrameric enzyme. Each pair dimer has two active sites which are located between the subunits. Each subunit consists of three domains that are related to each other by pseudo-3-fold symmetry. The essential divalent (Mg2+/Co2+) and monovalent (K+) metal ions and one of the product, Pi ions, were found in the active site from three separate structures.
About this Structure
1XRB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of S-adenosylmethionine synthetase., Takusagawa F, Kamitori S, Misaki S, Markham GD, J Biol Chem. 1996 Jan 5;271(1):136-47. PMID:8550549
Page seeded by OCA on Thu Mar 20 15:13:39 2008
