3c3d: Difference between revisions
New page: left|200px<br /><applet load="3c3d" size="350" color="white" frame="true" align="right" spinBox="true" caption="3c3d, resolution 2.50Å" /> '''Crystal structure of... |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:3c3d.jpg|left|200px]] | [[Image:3c3d.jpg|left|200px]] | ||
'''Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics | {{Structure | ||
|PDB= 3c3d |SIZE=350|CAPTION= <scene name='initialview01'>3c3d</scene>, resolution 2.50Å | |||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+402'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+B+402'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+C+402'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+D+402'>AC4</scene>, <scene name='pdbsite=AC5:Fo1+Binding+Site+For+Residue+A+401'>AC5</scene>, <scene name='pdbsite=AC6:Fo1+Binding+Site+For+Residue+B+401'>AC6</scene>, <scene name='pdbsite=AC7:Fo1+Binding+Site+For+Residue+C+401'>AC7</scene> and <scene name='pdbsite=AC8:Fo1+Binding+Site+For+Residue+D+401'>AC8</scene> | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FO1:'>FO1</scene> | |||
|ACTIVITY= | |||
|GENE= cofD, MM_1874 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192952 Methanosarcina mazei Go1]) | |||
}} | |||
'''Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46''' | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
3C3D is a [ | 3C3D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_mazei_go1 Methanosarcina mazei go1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3D OCA]. | ||
==Reference== | ==Reference== | ||
Molecular insights into the biosynthesis of the F420 coenzyme., Forouhar F, Abashidze M, Xu H, Grochowski LL, Seetharaman J, Hussain M, Kuzin A, Chen Y, Zhou W, Xiao R, Acton TB, Montelione GT, Galinier A, White RH, Tong L, J Biol Chem. 2008 Feb 5;. PMID:[http:// | Molecular insights into the biosynthesis of the F420 coenzyme., Forouhar F, Abashidze M, Xu H, Grochowski LL, Seetharaman J, Hussain M, Kuzin A, Chen Y, Zhou W, Xiao R, Acton TB, Montelione GT, Galinier A, White RH, Tong L, J Biol Chem. 2008 Feb 5;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18252724 18252724] | ||
[[Category: Methanosarcina mazei go1]] | [[Category: Methanosarcina mazei go1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 37: | Line 46: | ||
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi-2]] | [[Category: psi-2]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''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 19:02:23 2008'' |
Revision as of 20:02, 20 March 2008
| |||||||
, resolution 2.50Å | |||||||
---|---|---|---|---|---|---|---|
Sites: | , , , , , , and | ||||||
Ligands: | and | ||||||
Gene: | cofD, MM_1874 (Methanosarcina mazei Go1) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46
OverviewOverview
Coenzyme F420, a hydride carrier, is found in archaea and some bacteria and has crucial roles in methanogenesis, antibiotics biosynthesis, DNA repair, and activation of antitubercular compounds. CofD, 2-phospho-L-lactate transferase, catalyzes the last step in the biosynthesis of F420-0 (F420 without polyglutamate), by transferring the lactyl phosphate (LP) moiety of lactyl (2) diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (Fo). CofD is highly conserved among F420-producing organisms, and weak sequence homologs are also found in non-F420-producing organisms. This superfamily does not share any recognizable sequence conservation with other proteins. Here we report the first crystal structures of CofD-the free enzyme and two ternary complexes, with Fo and Pi or with Fo and GDP-from Methanosarcina mazei. The active site is located at the C-terminal end of a Rossmann-fold core, and three large insertions make significant contributions to the active site and dimer formation. The observed binding modes of Fo and GDP can explain known biochemical properties of CofD, and are also supported by our binding assays. The structures provide significant molecular insights into the biosynthesis of the F420 coenzyme. Large structural differences in the active site region of the non-F420-producing CofD homologs suggest that they catalyze a different biochemical reaction.
About this StructureAbout this Structure
3C3D is a Single protein structure of sequence from Methanosarcina mazei go1. Full crystallographic information is available from OCA.
ReferenceReference
Molecular insights into the biosynthesis of the F420 coenzyme., Forouhar F, Abashidze M, Xu H, Grochowski LL, Seetharaman J, Hussain M, Kuzin A, Chen Y, Zhou W, Xiao R, Acton TB, Montelione GT, Galinier A, White RH, Tong L, J Biol Chem. 2008 Feb 5;. PMID:18252724
Page seeded by OCA on Thu Mar 20 19:02:23 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Methanosarcina mazei go1
- Single protein
- Abashidze, M.
- Acton, T B.
- Chen, Y.
- Forouhar, F.
- Galinier, A.
- Grochowski, L L.
- Hussain, M.
- Kuzin, A P.
- Montelione, G T.
- NESG, Northeast Structural Genomics Consortium.
- Seetharaman, J.
- Tong, L.
- White, R H.
- Xiao, R.
- Xu, H.
- Zhou, W.
- FO1
- PO4
- Alpha-beta protein
- Magnesium
- Nesg
- Northeast structural genomics consortium
- Protein structure initiative
- Psi-2
- Structural genomic
- Transferase