1fux
From Proteopedia
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| - | [[Image:1fux.gif|left|200px]] | + | [[Image:1fux.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY''' | + | {{Structure |
| + | |PDB= 1fux |SIZE=350|CAPTION= <scene name='initialview01'>1fux</scene>, resolution 1.81Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FUX is a [ | + | 1FUX 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=1FUX OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein., Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H, J Mol Biol. 2001 Jul 13;310(3):617-34. PMID:[http:// | + | Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein., Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H, J Mol Biol. 2001 Jul 13;310(3):617-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11439028 11439028] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta protein]] | [[Category: beta protein]] | ||
| - | ''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 11:14:18 2008'' |
Revision as of 09:14, 20 March 2008
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| , resolution 1.81Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF E.COLI YBCL, A NEW MEMBER OF THE MAMMALIAN PEBP FAMILY
Overview
In rat and human cells, RKIP (previously known as PEBP) was characterized as an inhibitor of the MEK phosphorylation by Raf-1. In Escherichia coli, the genes ybhb and ybcl possibly encode two RKIP homologues while in the genomes of other bacteria and archaebacteria other homologous genes of RKIP have been found. The parallel between the cellular signaling mechanisms in eukaryotes and prokaryotes suggests that these bacterial proteins could be involved in the regulation of protein phosphorylation by kinases as well. We first showed that the proteins YBHB and YBCL were present in the cytoplasm and periplasm of E. coli, respectively, after which we determined their crystallographic structures. These structures verify that YBHB and YBCL belong to the same structural family as mammalian RKIP/PEBP proteins. The general fold and the anion binding site of these proteins are extremely well conserved between mammals and bacteria and suggest functional similarities. However, the bacterial proteins also exhibit some specific structural features, like a substrate binding pocket formed by the dimerization interface and the absence of cis peptide bonds. This structural variety should correspond to the recognition of multiple cellular partners.
About this Structure
1FUX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein., Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H, J Mol Biol. 2001 Jul 13;310(3):617-34. PMID:11439028
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