View source for 3agc


==F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana==
<StructureSection load='3agc' size='340' side='right'caption='[[3agc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3agc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AGC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RCC:3-{(2Z,3S,4S)-5-[(Z)-(4-ETHENYL-3-METHYL-5-OXO-1,5-DIHYDRO-2H-PYRROL-2-YLIDENE)METHYL]-2-[(5R)-2-[(3-ETHYL-5-FORMYL-4-METHYL-1H-PYRROL-2-YL)METHYL]-5-(METHOXYCARBONYL)-3-METHYL-4-OXO-4,5-DIHYDROCYCLOPENTA[B]PYRROL-6(1H)-YLIDENE]-4-METHYL-3,4-DIHYDRO-2H-PYRROL-3-YL}PROPANOIC+ACID'>RCC</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zxl|2zxl]], [[3aga|3aga]], [[3agb|3agb]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCCR, ACD2, At4g37000, C7A10_360 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Red_chlorophyll_catabolite_reductase Red chlorophyll catabolite reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.80 1.3.1.80] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3agc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3agc OCA], [https://pdbe.org/3agc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3agc RCSB], [https://www.ebi.ac.uk/pdbsum/3agc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3agc ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/RCCR_ARATH RCCR_ARATH]] Catalyzes the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary fluorescent catabolite (pFCC). Works in a two-step reaction with pheophorbide a oxygenase (PaO) by reducing the C20/C1 double bond of the intermediate, RCC.<ref>PMID:10743659</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/3agc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3agc ConSurf].
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== Publication Abstract from PubMed ==
Red chlorophyll catabolite reductase (RCCR) catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite (RCC), the catabolic intermediate produced in chlorophyll degradation. The crystal structure of substrate-free Arabidopsis thaliana RCCR (AtRCCR) demonstrated that RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase (FDBR) family. Here we have determined the crystal structures of RCC-bound AtRCCR, RCC-bound F218 V AtRCCR, and substrate-free F218 V AtRCCR, a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position. RCC is bound to the pocket between the beta-sheet and the C-terminal alpha-helices, as seen in substrate-bound FDBRs, but RCC binding to RCCR is much looser than substrate binding to FDBRs. The loose binding seems beneficial to the large conformational change in RCC upon reduction. Two conserved acidic residues, Glu154 and Asp291, sandwich the C20/C1 double bond of RCC, suggesting that these two residues are involved in site-specific reduction. The RCC in F218V AtRCCR rotates slightly compared with that in wild type to fill in the space generated by the substitution of Phe218 with valine. Concomitantly, the two carboxy groups of Glu154 and Asp291 move slightly away from the C20/C1 double bond. The geometrical arrangement of RCC and the carboxy groups of Glu154 and Asp291 in RCCR would appear to be essential for the stereospecificity of the RCCR reaction.

Crystal Structures of the Substrate-Bound Forms of Red Chlorophyll Catabolite Reductase: Implications for Site-Specific and Stereospecific Reaction.,Sugishima M, Okamoto Y, Noguchi M, Kohchi T, Tamiaki H, Fukuyama K J Mol Biol. 2010 Aug 19. PMID:20727901<ref>PMID:20727901</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3agc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Large Structures]]
[[Category: Red chlorophyll catabolite reductase]]
[[Category: Fukuyama, K]]
[[Category: Sugishima, M]]
[[Category: Chlorophyll catabolism]]
[[Category: Chlorophyll degradation]]
[[Category: Chloroplast]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Substrate-bound enzyme]]
[[Category: Transit peptide]]