3aer: Difference between revisions
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==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark== | ==Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark== | ||
<StructureSection load='3aer' size='340' side='right' caption='[[3aer]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3aer' size='340' side='right'caption='[[3aer]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3aer]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3aer]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AER FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=3aer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aer OCA], [https://pdbe.org/3aer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aer RCSB], [https://www.ebi.ac.uk/pdbsum/3aer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aer ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/BCHN_RHOCB BCHN_RHOCB] 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 NB-protein (BchN-BchB) is the catalytic component of the complex.[HAMAP-Rule:MF_00352]<ref>PMID:18358835</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/3aer_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/3aer_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fujita | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Kurisu | [[Category: Fujita Y]] | ||
[[Category: Muraki | [[Category: Kurisu G]] | ||
[[Category: Nomata | [[Category: Muraki N]] | ||
[[Category: Shiba | [[Category: Nomata J]] | ||
[[Category: Shiba T]] | |||