6l1h
From Proteopedia
(Difference between revisions)
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<StructureSection load='6l1h' size='340' side='right'caption='[[6l1h]], [[Resolution|resolution]] 2.41Å' scene=''> | <StructureSection load='6l1h' size='340' side='right'caption='[[6l1h]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6l1h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L1H OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6l1h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L1H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L1H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">por ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protochlorophyllide_reductase Protochlorophyllide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.33 1.3.1.33] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protochlorophyllide_reductase Protochlorophyllide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.33 1.3.1.33] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l1h OCA], [http://pdbe.org/6l1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l1h RCSB], [http://www.ebi.ac.uk/pdbsum/6l1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l1h ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q8DLC1_THEEB Q8DLC1_THEEB]] Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).[RuleBase:RU365001] | [[http://www.uniprot.org/uniprot/Q8DLC1_THEEB Q8DLC1_THEEB]] Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).[RuleBase:RU365001] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is the penultimate step of chlorophyll biosynthesis. In oxygenic photosynthetic bacteria, algae, and plants, this reaction can be catalyzed by the light-dependent Pchlide oxidoreductase (LPOR), a member of the short-chain dehydrogenase superfamily sharing a conserved Rossmann fold for NAD(P)H binding and the catalytic activity. Whereas modeling and simulation approaches have been used to study the catalytic mechanism of this light-driven reaction, key details of the LPOR structure remain unclear. We determined the crystal structures of LPOR from two cyanobacteria, Synechocystis sp. PCC 6803 and Thermosynechococcus elongatus Structural analysis defines the LPOR core fold, outlines the LPOR-NADPH interaction network, identifies the residues forming the substrate cavity and the proton-relay path, and reveals the role of the LPOR-specific loop. These findings provide a basis for understanding the structure-function relationships of the light-driven Pchlide reduction. | ||
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| + | Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.,Dong CS, Zhang WL, Wang Q, Li YS, Wang X, Zhang M, Liu L Proc Natl Acad Sci U S A. 2020 Mar 31. pii: 1920244117. doi:, 10.1073/pnas.1920244117. PMID:32234783<ref>PMID:32234783</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6l1h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Protochlorophyllide reductase]] | [[Category: Protochlorophyllide reductase]] | ||
| + | [[Category: Theeb]] | ||
[[Category: Dong, C]] | [[Category: Dong, C]] | ||
[[Category: Liu, L]] | [[Category: Liu, L]] | ||
Revision as of 07:12, 15 April 2020
Crystal structure of light-dependent protochlorophyllide oxidoreductase from Thermosynechococcus elongatus
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