1RLC: 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

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.
PDB ID: 1RLCDownload
MMDB ID: 51179
PDB Deposition Date: 1993/8/4
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1RLC: hexadecameric; determined by author and by software (PISA,PQS)
Molecular Components in 1RLC
Label Count Molecule
Proteins (16 molecules)
Ribulose 1,5 Bisphosphate Carboxylase/oxygenase (Large Chain)
Molecule annotation
Ribulose 1,5 Bisphosphate Carboxylase/oxygenase (Small Chain)
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB