1JQO

Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize

Summary for 1JQO

• Entry DOI: 10.2210/pdb1jqo/pdb
• Related: 1FIY 1JQN
• Descriptor: phosphoenolpyruvate carboxylase, SULFATE ION (2 entities in total)
• Functional Keywords: beta barrel, carbon dioxide fixation, lyase
• Biological source: Zea mays
• Cellular location: Cytoplasm: P04711
• Total number of polymer chains: 2
• Total formula weight: 219064.14

Authors

Matsumura, H.,Kai, Y. (deposition date: 2001-08-07, release date: 2003-01-14, Last modification date: 2024-03-13)

Primary citation

Matsumura, H.,Xie, Y.,Shirakata, S.,Inoue, T.,Yoshinaga, T.,Ueno, Y.,Izui, K.,Kai, Y.
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
Structure, 10:1721-1730, 2002

PubMed Abstract: Phosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the fixation of atmospheric CO(2) during C(4) photosynthesis. The crystal structure of C(4) form maize PEPC (ZmPEPC), the first structure of the plant PEPCs, has been determined at 3.0 A resolution. The structure includes a sulfate ion at the plausible binding site of an allosteric activator, glucose 6-phosphate. The crystal structure of E. coli PEPC (EcPEPC) complexed with Mn(2+), phosphoenolpyruvate analog (3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate), and an allosteric inhibitor, aspartate, has also been determined at 2.35 A resolution. Dynamic movements were found in the ZmPEPC structure, compared with the EcPEPC structure, around two loops near the active site. On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed.

PubMed: 12467579
DOI: 10.1016/S0969-2126(02)00913-9

Experimental method

X-RAY DIFFRACTION (3 Å)