1l3c
From Proteopedia
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|PDB= 1l3c |SIZE=350|CAPTION= <scene name='initialview01'>1l3c</scene>, resolution 2.31Å | |PDB= 1l3c |SIZE=350|CAPTION= <scene name='initialview01'>1l3c</scene>, resolution 2.31Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Mth146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | |GENE= Mth146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kxz|1KXZ]], [[1f38|1F38]], [[1l3b|1L3B]], [[1l3i|1L3I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3c OCA], [http://www.ebi.ac.uk/pdbsum/1l3c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l3c RCSB]</span> | ||
}} | }} | ||
| Line 36: | Line 39: | ||
[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:57:28 2008'' |
Revision as of 18:57, 30 March 2008
| |||||||
| , resolution 2.31Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Mth146 (Methanothermobacter thermautotrophicus) | ||||||
| Related: | 1KXZ, 1F38, 1L3B, 1L3I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MT0146, THE PRECORRIN-6Y METHYLTRANSFERASE (CBIT) HOMOLOG FROM M. THERMOAUTOTROPHICUM, C2 SPACEGROUP WITH SHORT CELL
Overview
The CbiT and CbiE enzymes participate in the biosynthesis of vitamin B12. They are fused together in some organisms to form a protein called CobL, which catalyzes two methylations and one decarboxylation on a precorrin intermediate. Because CbiE has sequence homology to canonical precorrin methyltransferases, CbiT was hypothesized to catalyze the decarboxylation. We herein present the crystal structure of MT0146, the CbiT homolog from Methanobacterium thermoautotrophicum. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and our 1.9 A cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that could accommodate a precorrin substrate. Therefore, MT0146/CbiT probably functions as a precorrin methyltransferase and represents the first enzyme identified with this activity that does not have the canonical precorrin methyltransferase fold.
About this Structure
1L3C is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase., Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF, Structure. 2002 Nov;10(11):1475-87. PMID:12429089
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