1xrb: Difference between revisions

Revision as of 14:16, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xrb.png

Template:STRUCTURE 1xrb

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)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)

Template:ABSTRACT PUBMED 8550549

About this StructureAbout this Structure

1XRB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Tue Jul 29 14:16:25 2008

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 {{STRUCTURE_1xrb|  PDB=1xrb  |  SCENE=  }}
-'''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)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8550549}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8550549 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8550549}}
 ==About this Structure==
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 [[Category: Takusagawa, F.]]
 [[Category: Methyltransferase]]
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