3c3d

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[[Image:3c3d.jpg|left|200px]]
[[Image:3c3d.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 3c3d |SIZE=350|CAPTION= <scene name='initialview01'>3c3d</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_3c3d", creates the "Structure Box" on the page.
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|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>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FO1:1-DEOXY-1-(8-HYDROXY-2,4-DIOXO-3,4-DIHYDROPYRIMIDO[4,5-B]QUINOLIN-10(2H)-YL)-D-RIBITOL'>FO1</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= cofD, MM_1874 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192952 Methanosarcina mazei Go1])
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-->
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|DOMAIN=
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{{STRUCTURE_3c3d| PDB=3c3d | SCENE= }}
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|RELATEDENTRY=[[3cgw|3CGW]], [[3c3e|3C3E]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c3d OCA], [http://www.ebi.ac.uk/pdbsum/3c3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c3d RCSB]</span>
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}}
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'''Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46'''
'''Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46'''
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[[Category: Xu, H.]]
[[Category: Xu, H.]]
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[[Category: Zhou, W.]]
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[[Category: alpha-beta protein]]
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[[Category: Alpha-beta protein]]
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[[Category: magnesium]]
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[[Category: Magnesium]]
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[[Category: nesg]]
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[[Category: Nesg]]
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[[Category: northeast structural genomics consortium]]
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[[Category: Northeast structural genomics consortium]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: psi-2]]
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[[Category: Psi-2]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:18:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:30:22 2008''
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Revision as of 18:18, 4 May 2008

Image:3c3d.jpg

Template:STRUCTURE 3c3d

Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46


Overview

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 Structure

3C3D is a Single protein structure of sequence from Methanosarcina mazei go1. Full crystallographic information is available from OCA.

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:18252724 Page seeded by OCA on Sun May 4 21:18:36 2008

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