1s4d
From Proteopedia
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| - | [[Image:1s4d.jpg|left|200px]] | + | [[Image:1s4d.jpg|left|200px]] |
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| - | '''Crystal Structure Analysis of the S-adenosyl-L-methionine dependent uroporphyrinogen-III C-methyltransferase SUMT''' | + | {{Structure |
| + | |PDB= 1s4d |SIZE=350|CAPTION= <scene name='initialview01'>1s4d</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= COBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 Pseudomonas denitrificans]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Analysis of the S-adenosyl-L-methionine dependent uroporphyrinogen-III C-methyltransferase SUMT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S4D is a [ | + | 1S4D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4D OCA]. |
==Reference== | ==Reference== | ||
| - | Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis., Vevodova J, Graham RM, Raux E, Schubert HL, Roper DI, Brindley AA, Ian Scott A, Roessner CA, Stamford NP, Elizabeth Stroupe M, Getzoff ED, Warren MJ, Wilson KS, J Mol Biol. 2004 Nov 19;344(2):419-33. PMID:[http:// | + | Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis., Vevodova J, Graham RM, Raux E, Schubert HL, Roper DI, Brindley AA, Ian Scott A, Roessner CA, Stamford NP, Elizabeth Stroupe M, Getzoff ED, Warren MJ, Wilson KS, J Mol Biol. 2004 Nov 19;344(2):419-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15522295 15522295] |
[[Category: Pseudomonas denitrificans]] | [[Category: Pseudomonas denitrificans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: uroporphyrinogen-iii methyltransferase]] | [[Category: uroporphyrinogen-iii methyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:16 2008'' |
Revision as of 12:00, 20 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | COBA (Pseudomonas denitrificans) | ||||||
| Activity: | Uroporphyrinogen-III C-methyltransferase, with EC number 2.1.1.107 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of the S-adenosyl-L-methionine dependent uroporphyrinogen-III C-methyltransferase SUMT
Overview
The crystallographic structure of the Pseudomonas denitrificans S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase (SUMT), which is encoded by the cobA gene, has been solved by molecular replacement to 2.7A resolution. SUMT is a branchpoint enzyme that plays a key role in the biosynthesis of modified tetrapyrroles by controlling flux to compounds such as vitamin B(12) and sirohaem, and catalysing the transformation of uroporphyrinogen III into precorrin-2. The overall topology of the enzyme is similar to that of the SUMT module of sirohaem synthase (CysG) and the cobalt-precorrin-4 methyltransferase CbiF and, as with the latter structures, SUMT has the product S-adenosyl-L-homocysteine bound in the crystal. The roles of a number of residues within the SUMT structure are discussed with respect to their conservation either across the broader family of cobalamin biosynthetic methyltransferases or within the sub-group of SUMT members. The D47N, L49A, F106A, T130A, Y183A and M184A variants of SUMT were generated by mutagenesis of the cobA gene, and tested for SAM binding and enzymatic activity. Of these variants, only D47N and L49A bound the co-substrate S-adenosyl-L-methionine. Consequently, all the mutants were severely restricted in their capacity to synthesise precorrin-2, although both the D47N and L49A variants produced significant quantities of precorrin-1, the monomethylated derivative of uroporphyrinogen III. The activity of these variants is interpreted with respect to the structure of the enzyme.
About this Structure
1S4D is a Single protein structure of sequence from Pseudomonas denitrificans. Full crystallographic information is available from OCA.
Reference
Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis., Vevodova J, Graham RM, Raux E, Schubert HL, Roper DI, Brindley AA, Ian Scott A, Roessner CA, Stamford NP, Elizabeth Stroupe M, Getzoff ED, Warren MJ, Wilson KS, J Mol Biol. 2004 Nov 19;344(2):419-33. PMID:15522295
Page seeded by OCA on Thu Mar 20 14:00:16 2008
Categories: Pseudomonas denitrificans | Single protein | Uroporphyrinogen-III C-methyltransferase | Brindley, A A. | Getzoff, E D. | Graham, R M. | Raux, E. | Roessner, C A. | Roper, D I. | Schubert, H L. | Scott, A I. | Stamford, N P.J. | Stroupe, M E. | Vevodova, J. | Warren, M J. | Wilson, K S. | GOL | SAH | Cobalamin | Sah | Sam | Tetrapyrrole biosynthesis | Uroporphyrinogen-iii methyltransferase
