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Crystal structure of the unactivated ribulose 1, 5‐bisphosphate carboxylase/oxygenase complexed with a transition state analog, 2‐carboxy‐D‐arabinitol 1, 5‐bisphosphate
Author(s) -
Zhang Kam Y.J.,
Cascio Duilio,
Eisenberg David
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030109
Subject(s) - transition state analog , ribulose 1,5 bisphosphate , stereochemistry , chemistry , oxygenase , active site , substrate analog , binding site , rubisco , ribulose , pyruvate carboxylase , crystal structure , nicotiana tabacum , enzyme , crystallography , biochemistry , gene
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 Å 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.