5dqr
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/7-hydroxymethyl_chlorophyll_a_reductase 7-hydroxymethyl chlorophyll a reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.7.2 1.17.7.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/7-hydroxymethyl_chlorophyll_a_reductase 7-hydroxymethyl chlorophyll a reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.7.2 1.17.7.2] </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=5dqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqr OCA], [http://pdbe.org/5dqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dqr RCSB], [http://www.ebi.ac.uk/pdbsum/5dqr 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=5dqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqr OCA], [http://pdbe.org/5dqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dqr RCSB], [http://www.ebi.ac.uk/pdbsum/5dqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dqr ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/HCAR_ARATH HCAR_ARATH]] Probable iron-sulfur flavoprotein that converts 7-hydroxymethyl chlorophyll a to chlorophyll a using ferredoxin as a reducing equivalent. Catalyzes the reduction of a hydroxymethyl group to a methyl group. Belongs to the chlorophyll catabolic enzymes (CCEs).<ref>PMID:21934147</ref> | [[http://www.uniprot.org/uniprot/HCAR_ARATH HCAR_ARATH]] Probable iron-sulfur flavoprotein that converts 7-hydroxymethyl chlorophyll a to chlorophyll a using ferredoxin as a reducing equivalent. Catalyzes the reduction of a hydroxymethyl group to a methyl group. Belongs to the chlorophyll catabolic enzymes (CCEs).<ref>PMID:21934147</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 7-Hydroxymethyl chlorophyll a reductase (HCAR) catalyzes the second half-reaction in chlorophyll b to chlorophyll a conversion. HCAR is required for the degradation of light-harvesting complexes and is necessary for efficient photosynthesis by balancing the chlorophyll a/b ratio. Reduction of the hydroxymethyl group uses redox cofactors [4Fe-4S] cluster and FAD to transfer electrons and is difficult because of the strong carbon-oxygen bond. Here, we report the crystal structure of Arabidopsis HCAR at 2.7-A resolution and reveal that two [4Fe-4S]clusters and one FAD within a very short distance form a consecutive electron pathway to the substrate pocket. In vitro kinetic analysis confirms the ferredoxin-dependent electron transport chain, thus supporting a proton-activated electron transfer mechanism. HCAR resembles a partial reconstruction of an archaeal F420-reducing [NiFe] hydrogenase, which suggests a common mode of efficient proton-coupled electron transfer through conserved cofactor arrangements. Furthermore, the trimeric form of HCAR provides a biological clue of its interaction with light-harvesting complex II. | ||
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| + | Crystal Structure and Catalytic Mechanism of 7-Hydroxymethyl Chlorophyll a Reductase.,Wang X, Liu L J Biol Chem. 2016 Jun 17;291(25):13349-59. doi: 10.1074/jbc.M116.720342. Epub, 2016 Apr 12. PMID:27072131<ref>PMID:27072131</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5dqr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:30, 12 July 2016
The crystal structure of Arabidopsis 7-hydroxymethyl chlorophyll a reductase (HCAR)
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