1rlc
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of unactivated ribulose 1,5-bisphosphate | + | 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== | ==About this Structure== | ||
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[[Category: Cascio, D.]] | [[Category: Cascio, D.]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
| - | [[Category: Zhang, K | + | [[Category: Zhang, K Y.J.]] |
[[Category: CAP]] | [[Category: CAP]] | ||
[[Category: lyase(carbon-carbon)]] | [[Category: lyase(carbon-carbon)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:06 2008'' |
Revision as of 12:52, 21 February 2008
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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
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.
About 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.
Reference
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
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