1fiy: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1fiy.gif|left|200px]] | [[Image:1fiy.gif|left|200px]] | ||
'''THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION''' | {{Structure | ||
|PDB= 1fiy |SIZE=350|CAPTION= <scene name='initialview01'>1fiy</scene>, resolution 2.8Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1FIY is a [ | 1FIY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9927652 9927652] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoenolpyruvate carboxylase]] | [[Category: Phosphoenolpyruvate carboxylase]] | ||
| Line 27: | Line 36: | ||
[[Category: phosphoenolpyruvate]] | [[Category: phosphoenolpyruvate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:41 2008'' | ||
Revision as of 09:09, 20 March 2008
| |||||||||||||
| 1fiy, resolution 2.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ASP | ||||||||||||
| Activity: | Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31 | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 11:09:41 2008
