1fx3
From Proteopedia
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| - | [[Image:1fx3.gif|left|200px]] | + | [[Image:1fx3.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF H. INFLUENZAE SECB''' | + | {{Structure |
| + | |PDB= 1fx3 |SIZE=350|CAPTION= <scene name='initialview01'>1fx3</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF H. INFLUENZAE SECB''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FX3 is a [ | + | 1FX3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX3 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the bacterial protein export chaperone secB., Xu Z, Knafels JD, Yoshino K, Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:[http:// | + | Crystal structure of the bacterial protein export chaperone secB., Xu Z, Knafels JD, Yoshino K, Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11101901 11101901] |
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: translocation]] | [[Category: translocation]] | ||
| - | ''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 11:15:10 2008'' |
Revision as of 09:15, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF H. INFLUENZAE SECB
Overview
SecB is a bacterial molecular chaperone involved in mediating translocation of newly synthesized polypeptides across the cytoplasmic membrane of bacteria. The crystal structure of SecB from Haemophilus influenzae shows that the molecule is a tetramer organized as a dimer of dimers. Two long channels run along the side of the molecule. These are bounded by flexible loops and lined with conserved hydrophobic amino acids, which define a suitable environment for binding non-native polypeptides. The structure also reveals an acidic region on the top surface of the molecule, several residues of which have been implicated in binding to SecA, its downstream target.
About this Structure
1FX3 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the bacterial protein export chaperone secB., Xu Z, Knafels JD, Yoshino K, Nat Struct Biol. 2000 Dec;7(12):1172-7. PMID:11101901
Page seeded by OCA on Thu Mar 20 11:15:10 2008
