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

Summary for 1RLC

• Entry DOI: 10.2210/pdb1rlc/pdb
• Descriptor: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE CHAIN), RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL CHAIN), 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE (3 entities in total)
• Functional Keywords: lyase(carbon-carbon)
• Biological source: Nicotiana tabacum (common tobacco); More
• Cellular location: Plastid, chloroplast: P69249
• Total number of polymer chains: 2
• Total formula weight: 67896.79

Authors

Zhang, K.Y.J.,Cascio, D.,Eisenberg, D. (deposition date: 1993-08-04, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Zhang, K.Y.,Cascio, D.,Eisenberg, D.
Crystal structure of the unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate.
Protein Sci., 3:64-69, 1994

PubMed Abstract: 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.

PubMed: 8142899

Experimental method

X-RAY DIFFRACTION (2.7 Å)