1jay

From Proteopedia

(Difference between revisions)

Revision as of 08:55, 17 January 2018

Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) with its substrates bound

Structural highlights

1jay is a 2 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1jax
Gene:	AF0892 (ARCFL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[F42NO_ARCFU] Catalyzes the reversible reduction of NADP(+) by F420H(2). In this reaction the proS hydrogen at C5 of F420 is transferred into the proS position at C4 of NADPH. Has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cofactor F420 is a 5'-deazaflavin derivative first discovered in methanogenic archaea but later found also to be present in some bacteria. As a coenzyme, it is involved in hydride transfer reactions and as a prosthetic group in the DNA photolyase reaction. We report here for the first time on the crystal structure of an F420-dependent oxidoreductase bound with F420. The structure of F420H2:NADP+ oxidoreductase resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer. Comparison of the structures bound with and without substrates reveals that of the two substrates NADP has to bind first, the binding being associated with an induced fit.

Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound.,Warkentin E, Mamat B, Sordel-Klippert M, Wicke M, Thauer RK, Iwata M, Iwata S, Ermler U, Shima S EMBO J. 2001 Dec 3;20(23):6561-9. PMID:11726492^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Warkentin E, Mamat B, Sordel-Klippert M, Wicke M, Thauer RK, Iwata M, Iwata S, Ermler U, Shima S. Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound. EMBO J. 2001 Dec 3;20(23):6561-9. PMID:11726492 doi:10.1093/emboj/20.23.6561
↑ Warkentin E, Mamat B, Sordel-Klippert M, Wicke M, Thauer RK, Iwata M, Iwata S, Ermler U, Shima S. Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound. EMBO J. 2001 Dec 3;20(23):6561-9. PMID:11726492 doi:10.1093/emboj/20.23.6561

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jay"

@@ Line 1: / Line 1: @@
 ==Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) with its substrates bound==
 <StructureSection load='1jay' size='340' side='right' caption='[[1jay]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jax|1jax]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF0892 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jay OCA], [http://pdbe.org/1jay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jay RCSB], [http://www.ebi.ac.uk/pdbsum/1jay PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jay OCA], [http://pdbe.org/1jay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jay RCSB], [http://www.ebi.ac.uk/pdbsum/1jay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jay ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/1jay_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/1jay_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1jay

From Proteopedia

Revision as of 08:55, 17 January 2018

Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) with its substrates bound

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox