1v9a: Difference between revisions
New page: left|200px<br /><applet load="1v9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v9a, resolution 2.00Å" /> '''Crystal structure of... |
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[[Image:1v9a.gif|left|200px]]<br /><applet load="1v9a" size=" | [[Image:1v9a.gif|left|200px]]<br /><applet load="1v9a" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1v9a, resolution 2.00Å" /> | caption="1v9a, resolution 2.00Å" /> | ||
'''Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine'''<br /> | '''Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine'''<br /> | ||
==Overview== | ==Overview== | ||
Uroporphyrinogen-III C-methyltransferase from Thermus thermophilus is a | Uroporphyrinogen-III C-methyltransferase from Thermus thermophilus is a multifunctional protein responsible for two of the eight S-adenosyl-methionine-dependent methylations of the corrin ring during vitamin B(12) synthesis. The structure of this protein has been solved to 2.0 A resolution in both the apo and cofactor-bound form. The monomer consists of two domains, A and B, each consisting of a five-stranded beta-sheet and two or three alpha-helices, with the cofactor bound at the interface. The biological unit is the dimer found in the asymmetric unit. This dimer is related by a non-crystallographic twofold such that two B domains combine to form a long ten-stranded beta-sheet. When compared with solved related structures, this structure shows clear differences in the region involved in cofactor and substrate binding, affirming the role of several previously implicated residues and questioning others. The solved related structures are characterized by an exposed active site. The T. thermophilus structure has this site restricted by the interaction of a flexible loop structure with a highly conserved residue, suggesting a mechanistic role. This structure represents the ;closed' form of the protein. | ||
==About this Structure== | ==About this Structure== | ||
1V9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with FLC and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uroporphyrinogen-III_C-methyltransferase Uroporphyrinogen-III C-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.107 2.1.1.107] Full crystallographic information is available from [http:// | 1V9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uroporphyrinogen-III_C-methyltransferase Uroporphyrinogen-III C-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.107 2.1.1.107] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9A OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Uroporphyrinogen-III C-methyltransferase]] | [[Category: Uroporphyrinogen-III C-methyltransferase]] | ||
[[Category: Kitao, T.]] | [[Category: Kitao, T.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Rehse, P | [[Category: Rehse, P H.]] | ||
[[Category: Tahirov, T | [[Category: Tahirov, T H.]] | ||
[[Category: FLC]] | [[Category: FLC]] | ||
[[Category: SAH]] | [[Category: SAH]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:56 2008'' | ||
Revision as of 16:33, 21 February 2008
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Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine
OverviewOverview
Uroporphyrinogen-III C-methyltransferase from Thermus thermophilus is a multifunctional protein responsible for two of the eight S-adenosyl-methionine-dependent methylations of the corrin ring during vitamin B(12) synthesis. The structure of this protein has been solved to 2.0 A resolution in both the apo and cofactor-bound form. The monomer consists of two domains, A and B, each consisting of a five-stranded beta-sheet and two or three alpha-helices, with the cofactor bound at the interface. The biological unit is the dimer found in the asymmetric unit. This dimer is related by a non-crystallographic twofold such that two B domains combine to form a long ten-stranded beta-sheet. When compared with solved related structures, this structure shows clear differences in the region involved in cofactor and substrate binding, affirming the role of several previously implicated residues and questioning others. The solved related structures are characterized by an exposed active site. The T. thermophilus structure has this site restricted by the interaction of a flexible loop structure with a highly conserved residue, suggesting a mechanistic role. This structure represents the ;closed' form of the protein.
About this StructureAbout this Structure
1V9A is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Active as Uroporphyrinogen-III C-methyltransferase, with EC number 2.1.1.107 Full crystallographic information is available from OCA.
ReferenceReference
Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilus., Rehse PH, Kitao T, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):913-9. Epub 2005, Jun 24. PMID:15983414
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