1fx3: Difference between revisions

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[[Image:1fx3.~~gif~~|left|200px]]

[[Image:1fx3.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF H. INFLUENZAE SECB~~'''~~

===CRYSTAL STRUCTURE OF H. INFLUENZAE SECB===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11101901}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11101901 is the PubMed ID number.

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==About this Structure==

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[[Category: Protein trasnport]]

[[Category: Translocation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:51:55 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:04:41 2008''

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-[[Image:1fx3.gif|left|200px]]
+{{Seed}}
+[[Image:1fx3.png|left|200px]]
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 {{STRUCTURE_1fx3|  PDB=1fx3  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF H. INFLUENZAE SECB'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11101901}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11101901 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11101901}}
 ==About this Structure==
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 [[Category: Protein trasnport]]
 [[Category: Translocation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:51:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:04:41 2008''