1fx3: Difference between revisions

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[[Image:1fx3.gif|left|200px]]<br /><applet load="1fx3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fx3.gif|left|200px]]<br /><applet load="1fx3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fx3, resolution 2.50Å" />

'''CRYSTAL STRUCTURE OF H. INFLUENZAE SECB'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FX3 OCA].

1FX3 is a [http://en.wikipedia.org/wiki/Single_protein 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==

Line 13:

[[Category: Haemophilus influenzae]]

[[Category: Single protein]]

[[Category: Knafels, J.D.]]

[[Category: Knafels, J D.]]

[[Category: Xu, Z.]]

[[Category: Yoshino, K.]]

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[[Category: translocation]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:25:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:36 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1fx3.gif|left|200px]]<br /><applet load="1fx3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fx3.gif|left|200px]]<br /><applet load="1fx3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fx3, resolution 2.50&Aring;" />
 '''CRYSTAL STRUCTURE OF H. INFLUENZAE SECB'''<br />
 ==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.
+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==
-FX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FX3 OCA].
+FX3 is a [http://en.wikipedia.org/wiki/Single_protein 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==
@@ Line 13: / Line 13: @@
 [[Category: Haemophilus influenzae]]
 [[Category: Single protein]]
-[[Category: Knafels, J.D.]]
+[[Category: Knafels, J D.]]
 [[Category: Xu, Z.]]
 [[Category: Yoshino, K.]]
@@ Line 19: / Line 19: @@
 [[Category: translocation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:25:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:36 2008''