1xrb
From Proteopedia
(New page: 200px<br /><applet load="1xrb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xrb, resolution 3.0Å" /> '''S-ADENOSYLMETHIONINE ...) |
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| - | [[Image:1xrb.jpg|left|200px]]<br /><applet load="1xrb" size=" | + | [[Image:1xrb.jpg|left|200px]]<br /><applet load="1xrb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xrb, resolution 3.0Å" /> | caption="1xrb, resolution 3.0Å" /> | ||
'''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)'''<br /> | '''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)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of S-adenosylmethionine synthetase (MAT, ATP:L-methionine | + | 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== | ==About this Structure== | ||
| - | 1XRB 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, MG 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:// | + | 1XRB 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=MG:'>MG</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=1XRB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kamitori, S.]] | [[Category: Kamitori, S.]] | ||
| - | [[Category: Markham, G | + | [[Category: Markham, G D.]] |
[[Category: Misaki, S.]] | [[Category: Misaki, S.]] | ||
[[Category: Takusagawa, F.]] | [[Category: Takusagawa, F.]] | ||
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[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:51 2008'' |
Revision as of 13:57, 21 February 2008
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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 with , and as ligands. Active as Methionine adenosyltransferase, with EC number 2.5.1.6 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
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