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3fwy

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Revision as of 06:51, 1 November 2017

Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein

Structural highlights

3fwy is a 2 chain structure with sequence from Rhos4. This structure supersedes the now removed PDB entry 3end. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	bchL, RHOS4_18930, RSP_0288 (RHOS4)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BCHL_RHOS4] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.[HAMAP-Rule:MF_00355]^[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

The L protein (BchL) of the dark-operative protochlorophyllide reductase (DPOR) from Rhodobacter sphaeroides has been purified from an Azotobacter vinelandii expression system; its interaction with nucleotides has been examined, and the X-ray structure of the protein has been determined with bound MgADP to 1.6 A resolution. DPOR catalyzes the reduction of protochlorophyllide to chlorophyllide, a reaction critical to the biosynthesis of bacteriochlorophylls. The DPOR holoenzyme is comprised of two component proteins, the dimeric BchL protein and the heterotetrameric BchN/BchB protein. The DPOR component proteins share significant overall similarities with the nitrogenase Fe protein (NifH) and the MoFe (NifDK) protein, the enzyme system responsible for reduction of dinitrogen to ammonia. Here, BchL was expressed in A. vinelandii and purified to homogeneity using an engineered polyhistidine tag. The purified, recombinant BchL was found to contain 3.6 mol of Fe/mol of BchL homodimer, consistent with the presence of a [4Fe-4S] cluster and analogous to the [4Fe-4S] cluster present in the Fe protein. The MgATP- and MgADP-induced conformational changes in BchL were examined by an Fe chelation assay and found to be distinctly different from the nucleotide-stimulated Fe release observed for the Fe protein. The recombinant BchL was crystallized with bound MgADP, and the structure was determined to 1.6 A resolution. BchL is found to share overall structural similarity with the nitrogenase Fe protein, including the subunit bridging [4Fe-4S] cluster and nucleotide binding sites. Despite the high level of structural similarity, however, BchL is found to be incapable of substituting for the Fe protein in a nitrogenase substrate reduction assay. The newly determined structure of BchL and its comparison to its close homologue, the nitrogenase Fe protein, provide the basis for understanding how these highly related proteins can discriminate between their respective functions in microbial systems where each must function simultaneously.

Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein.,Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW Biochemistry. 2008 Nov 12. PMID:19006326^[2]

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

References

↑ Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW. Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein. Biochemistry. 2008 Nov 12. PMID:19006326 doi:10.1021/bi801058r
↑ Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW. Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein. Biochemistry. 2008 Nov 12. PMID:19006326 doi:10.1021/bi801058r

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/3fwy"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein==
 <StructureSection load='3fwy' size='340' side='right' caption='[[3fwy]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bchL, RHOS4_18930, RSP_0288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4])</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=3fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwy OCA], [http://pdbe.org/3fwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fwy RCSB], [http://www.ebi.ac.uk/pdbsum/3fwy 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=3fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwy OCA], [http://pdbe.org/3fwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fwy RCSB], [http://www.ebi.ac.uk/pdbsum/3fwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fwy ProSAT]</span></td></tr>
 </table>
 == Function ==

3fwy

From Proteopedia

Revision as of 06:51, 1 November 2017

Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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