1o92
From Proteopedia
(New page: 200px<br /> <applet load="1o92" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o92, resolution 3.19Å" /> '''METHIONINE ADENOSYL...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1O92 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with PO4, MG, K, AMB and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1O92 OCA]]. | + | 1O92 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with PO4, MG, K, AMB and ADP 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]]. Structure known Active Site: ADP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O92 OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism., Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J, J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12888348 12888348] | Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism., Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J, J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12888348 12888348] | ||
| + | [[Category: Methionine adenosyltransferase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:01:41 2007'' |
Revision as of 11:56, 30 October 2007
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METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ADP AND A L-METHIONINE ANALOGOUS
Overview
Methionine adenosyltransferases (MATs) are a family of enzymes in charge, of synthesising S-adenosylmethionine (SAM), the most important methyl, donor present in living organisms. These enzymes use methionine and ATP as, reaction substrates, which react in a S(N)2 fashion where the sulphur atom, from methionine attacks C5' from ATP while triphosphate chain is cleaved., A MAT liver specific isoenzyme has been detected, which exists in two, distinct oligomeric forms, a dimer (MAT III) and a tetramer (MAT I). Our, previously reported crystal structure of MAT I complexed with an inhibitor, led to the identification of the methionine-binding site. We present here, the results obtained from the complex of MAT I with a competitive, inhibitor of methionine, (2S,4S)-amino-4,5-epoxypentanoic acid ... [(full description)]
About this Structure
1O92 is a [Single protein] structure of sequence from [Rattus norvegicus] with PO4, MG, K, AMB and ADP as [ligands]. Active as [Methionine adenosyltransferase], with EC number [2.5.1.6]. Structure known Active Site: ADP. Full crystallographic information is available from [OCA].
Reference
Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism., Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J, J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:12888348
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