1rlc

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1rlc, resolution 2.70Å ()
Ligands:
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

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

Publication Abstract from PubMed

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.

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

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

About this Structure

1rlc is a 2 chain structure with sequence from Nicotiana tabacum. The November 2000 RCSB PDB Molecule of the Month feature on Rubisco by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_11. Full crystallographic information is available from OCA.

See Also

Reference

  • Zhang KY, 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. 1994 Jan;3(1):64-9. PMID:8142899

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