2wvw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:37, 12 January 2022) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
==Cryo-EM structure of the RbcL-RbcX complex==
==Cryo-EM structure of the RbcL-RbcX complex==
-
<StructureSection load='2wvw' size='340' side='right' caption='[[2wvw]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
+
<SX load='2wvw' size='340' side='right' viewer='molstar' caption='[[2wvw]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2wvw]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Anasc Anasc] and [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WVW FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2wvw]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Anasc Anasc] and [https://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVW FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rsc|1rsc]], [[1rbl|1rbl]]</td></tr>
+
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rsc|1rsc]], [[1rbl|1rbl]]</div></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2wvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvw OCA], [http://pdbe.org/2wvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wvw RCSB], [http://www.ebi.ac.uk/pdbsum/2wvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvw ProSAT]</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=2wvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvw OCA], [https://pdbe.org/2wvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvw RCSB], [https://www.ebi.ac.uk/pdbsum/2wvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
+
[[https://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wvw_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wvw_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
Line 31: Line 31:
==See Also==
==See Also==
-
*[[RuBisCO|RuBisCO]]
+
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
-
</StructureSection>
+
</SX>
[[Category: Anacystis nidulans]]
[[Category: Anacystis nidulans]]
[[Category: Anasc]]
[[Category: Anasc]]
 +
[[Category: Large Structures]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Beckmann, R]]
[[Category: Beckmann, R]]

Current revision

Cryo-EM structure of the RbcL-RbcX complex

2wvw, resolution 9.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools