1rlc: Difference between revisions

Revision as of 15:52, 21 February 2008

CRYSTAL STRUCTURE OF THE UNACTIVATED RIBULOSE 1, 5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE COMPLEXED WITH A TRANSITION STATE ANALOG, 2-CARBOXY-D-ARABINITOL 1,5-BISPHOSPHATE

OverviewOverview

The crystal structure of unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate, was determined to 2.7 A resolution by X-ray crystallography. The transition state analog binds at the active site in an extended conformation. As compared to the binding of the same analog in the activated enzyme, the analog binds in a reverse orientation. The active site Lys 201 is within hydrogen bonding distance of the carboxyl oxygen of the analog. Loop 6 (residues 330-339) remains open and flexible upon binding of the analog in the unactivated enzyme, in contrast to the closed and ordered loop 6 in the activated enzyme complex. The transition state analog is exposed to solvent due to the open conformation of loop 6.

About this StructureAbout this Structure

1RLC is a Protein complex structure of sequences from Nicotiana tabacum with as ligand. The following page contains interesting information on the relation of 1RLC with [Rubisco]. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate., Zhang KY, Cascio D, Eisenberg D, Protein Sci. 1994 Jan;3(1):64-9. PMID:8142899

Page seeded by OCA on Thu Feb 21 14:52:06 2008

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OCA

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 ==Overview==
-The crystal structure of unactivated ribulose 1,5-bisphosphate, carboxylase/oxygenase from Nicotiana tabacum complexed with a transition, state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate, was determined to, 2.7 A resolution by X-ray crystallography. The transition state analog, binds at the active site in an extended conformation. As compared to the, binding of the same analog in the activated enzyme, the analog binds in a, reverse orientation. The active site Lys 201 is within hydrogen bonding, distance of the carboxyl oxygen of the analog. Loop 6 (residues 330-339), remains open and flexible upon binding of the analog in the unactivated, enzyme, in contrast to the closed and ordered loop 6 in the activated, enzyme complex. The transition state analog is exposed to solvent due to, the open conformation of loop 6.
+The crystal structure of unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate, was determined to 2.7 A resolution by X-ray crystallography. The transition state analog binds at the active site in an extended conformation. As compared to the binding of the same analog in the activated enzyme, the analog binds in a reverse orientation. The active site Lys 201 is within hydrogen bonding distance of the carboxyl oxygen of the analog. Loop 6 (residues 330-339) remains open and flexible upon binding of the analog in the unactivated enzyme, in contrast to the closed and ordered loop 6 in the activated enzyme complex. The transition state analog is exposed to solvent due to the open conformation of loop 6.
 ==About this Structure==
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 [[Category: Cascio, D.]]
 [[Category: Eisenberg, D.]]
-[[Category: Zhang, K.Y.J.]]
+[[Category: Zhang, K Y.J.]]
 [[Category: CAP]]
 [[Category: lyase(carbon-carbon)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:48:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:06 2008''