1xrc: Difference between revisions

Revision as of 16:58, 21 February 2008

CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE

OverviewOverview

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 StructureAbout this Structure

1XRC is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Methionine adenosyltransferase, with EC number 2.5.1.6 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 Thu Feb 21 15:57:56 2008

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OCA

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-[[Image:1xrc.jpg|left|200px]]<br /><applet load="1xrc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1xrc.jpg|left|200px]]<br /><applet load="1xrc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1xrc, resolution 3.0&Aring;" />
 '''CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE'''<br />
 ==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 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==
-XRC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, CO and K as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XRC OCA].
+XRC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRC OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Kamitori, S.]]
-[[Category: Markham, G.D.]]
+[[Category: Markham, G D.]]
 [[Category: Misaki, S.]]
 [[Category: Takusagawa, F.]]
@@ Line 23: / Line 23: @@
 [[Category: methyltransferase]]
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