1fiy
From Proteopedia
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|PDB= 1fiy |SIZE=350|CAPTION= <scene name='initialview01'>1fiy</scene>, resolution 2.8Å | |PDB= 1fiy |SIZE=350|CAPTION= <scene name='initialview01'>1fiy</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene> | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fiy OCA], [http://www.ebi.ac.uk/pdbsum/1fiy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fiy RCSB]</span> | ||
}} | }} | ||
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[[Category: Terada, K.]] | [[Category: Terada, K.]] | ||
[[Category: Yoshinaga, T.]] | [[Category: Yoshinaga, T.]] | ||
| - | [[Category: ASP]] | ||
[[Category: carboxylase]] | [[Category: carboxylase]] | ||
[[Category: complex (lyase/inhibitor)]] | [[Category: complex (lyase/inhibitor)]] | ||
[[Category: phosphoenolpyruvate]] | [[Category: phosphoenolpyruvate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:47 2008'' |
Revision as of 17:23, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION
Overview
The crystal structure of phosphoenolpyruvate carboxylase (PEPC; EC 4. 1.1.31) has been determined by x-ray diffraction methods at 2.8-A resolution by using Escherichia coli PEPC complexed with L-aspartate, an allosteric inhibitor of all known PEPCs. The four subunits are arranged in a "dimer-of-dimers" form with respect to subunit contact, resulting in an overall square arrangement. The contents of alpha-helices and beta-strands are 65% and 5%, respectively. All of the eight beta-strands, which are widely dispersed in the primary structure, participate in the formation of a single beta-barrel. Replacement of a conserved Arg residue (Arg-438) in this linkage with Cys increased the tendency of the enzyme to dissociate into dimers. The location of the catalytic site is likely to be near the C-terminal side of the beta-barrel. The binding site for L-aspartate is located about 20 A away from the catalytic site, and four residues (Lys-773, Arg-832, Arg-587, and Asn-881) are involved in effector binding. The participation of Arg-587 is unexpected, because it is known to be catalytically essential. Because this residue is in a highly conserved glycine-rich loop, which is characteristic of PEPC, L-aspartate seemingly causes inhibition by removing this glycine-rich loop from the catalytic site. There is another mobile loop from Lys-702 to Gly-708 that is missing in the crystal structure. The importance of this loop in catalytic activity was also shown. Thus, the crystal-structure determination of PEPC revealed two mobile loops bearing the enzymatic functions and accompanying allosteric inhibition by L-aspartate.
About this Structure
1FIY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition., Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, Kihara A, Tsumura K, Izui K, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):823-8. PMID:9927652
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