1rld

From Proteopedia

(Difference between revisions)

Revision as of 10:14, 15 September 2021

SOLID-STATE PHASE TRANSITION IN THE CRYSTAL STRUCTURE OF RIBULOSE 1,5-BIPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE

Structural highlights

1rld is a 4 chain structure with sequence from American tobacco. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RBL_TOBAC] 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] [RBS_TOBAC] 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. Both reactions occur simultaneously and in competition at the same active site.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure is described of ribulose 1,5-bisphosphate carboxylase/oxygenase in a new crystal form. This new form (form V) was obtained from a previously known crystal form (form III) through a solid-state phase transition. The solid-state phase transition was brought about by transferring the crystal from a high-salt low-pH mother liquor to a low-salt high-pH synthetic mother liquor. The interplay of electrostatic repulsion and osmotic pressure induced a unit-cell shrinkage of 24 A along the c axis and expansion of 4 A along the a and b axes. The space group also changed from I422 to I4. The new crystal form was shown to be more resistant to X-ray radiation damage, which suggests the effect of crystal stabilization by non-penetrating molecules. The structure of ribulose 1,5-bisphosphate carboxylase/oxygenase in the new crystal form is compared with that of the old crystal form.

Solid-state phase transition in the crystal structure of ribulose 1,5-bisphosphate carboxylase/oxygenase.,Zhang KY, Eisenberg D Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):258-62. PMID:15299436^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhang KY, Eisenberg D. Solid-state phase transition in the crystal structure of ribulose 1,5-bisphosphate carboxylase/oxygenase. Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):258-62. PMID:15299436 doi:10.1107/S090744499301306X

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rld"

Categories: American tobacco | Large Structures | Ribulose-bisphosphate carboxylase | Eisenberg, D | Zhang, K Y.J

@@ Line 3: / Line 3: @@
 <StructureSection load='1rld' size='340' side='right'caption='[[1rld]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rld]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RLD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rld]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLD FirstGlance]. <br>
-</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>
+</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=1rld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rld OCA], [http://pdbe.org/1rld PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rld RCSB], [http://www.ebi.ac.uk/pdbsum/1rld PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rld 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=1rld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rld OCA], [https://pdbe.org/1rld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rld RCSB], [https://www.ebi.ac.uk/pdbsum/1rld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rld ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RBL_TOBAC RBL_TOBAC]] 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] [[http://www.uniprot.org/uniprot/RBS_TOBAC RBS_TOBAC]] 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. Both reactions occur simultaneously and in competition at the same active site.
+[[https://www.uniprot.org/uniprot/RBL_TOBAC RBL_TOBAC]] 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/RBS_TOBAC RBS_TOBAC]] 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. Both reactions occur simultaneously and in competition at the same active site.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[RuBisCO|RuBisCO]]
+*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 == References ==
 <references/>

1rld

From Proteopedia

Revision as of 10:14, 15 September 2021

SOLID-STATE PHASE TRANSITION IN THE CRYSTAL STRUCTURE OF RIBULOSE 1,5-BIPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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Proteopedia Page Contributors and Editors (what is this?)

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