1b0u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b0u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0u, resolution 1.50&Aring;" /> '''ATP-BINDING SUBUNIT ...)
Line 1: Line 1:
-
[[Image:1b0u.jpg|left|200px]]<br /><applet load="1b0u" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1b0u.jpg|left|200px]]<br /><applet load="1b0u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b0u, resolution 1.50&Aring;" />
caption="1b0u, resolution 1.50&Aring;" />
'''ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM'''<br />
'''ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM'''<br />
==Overview==
==Overview==
-
ABC transporters (also known as traffic ATPases) form a large family of, proteins responsible for the translocation of a variety of compounds, across membranes of both prokaryotes and eukaryotes. The recently, completed Escherichia coli genome sequence revealed that the largest, family of paralogous E. coli proteins is composed of ABC transporters., Many eukaryotic proteins of medical significance belong to this family, such as the cystic fibrosis transmembrane conductance regulator (CFTR), the P-glycoprotein (or multidrug-resistance protein) and the heterodimeric, transporter associated with antigen processing (Tap1-Tap2). Here we report, the crystal structure at 1.5 A resolution of HisP, the ATP-binding subunit, of the histidine permease, which is an ABC transporter from Salmonella, typhimurium. We correlate the details of this structure with the, biochemical, genetic and biophysical properties of the wild-type and, several mutant HisP proteins. The structure provides a basis for, understanding properties of ABC transporters and of defective CFTR, proteins.
+
ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety of compounds across membranes of both prokaryotes and eukaryotes. The recently completed Escherichia coli genome sequence revealed that the largest family of paralogous E. coli proteins is composed of ABC transporters. Many eukaryotic proteins of medical significance belong to this family, such as the cystic fibrosis transmembrane conductance regulator (CFTR), the P-glycoprotein (or multidrug-resistance protein) and the heterodimeric transporter associated with antigen processing (Tap1-Tap2). Here we report the crystal structure at 1.5 A resolution of HisP, the ATP-binding subunit of the histidine permease, which is an ABC transporter from Salmonella typhimurium. We correlate the details of this structure with the biochemical, genetic and biophysical properties of the wild-type and several mutant HisP proteins. The structure provides a basis for understanding properties of ABC transporters and of defective CFTR proteins.
==About this Structure==
==About this Structure==
-
1B0U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with CL and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B0U OCA].
+
1B0U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0U OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Ames, G.F.L.]]
+
[[Category: Ames, G F.L.]]
-
[[Category: Hung, L.W.]]
+
[[Category: Hung, L W.]]
-
[[Category: Kim, S.H.]]
+
[[Category: Kim, S H.]]
-
[[Category: Liu, P.Q.]]
+
[[Category: Liu, P Q.]]
[[Category: Nikaido, K.]]
[[Category: Nikaido, K.]]
-
[[Category: Wang, I.X.]]
+
[[Category: Wang, I X.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: CL]]
[[Category: CL]]
Line 25: Line 25:
[[Category: transport protein]]
[[Category: transport protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:15:54 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:26 2008''

Revision as of 09:50, 21 February 2008


1b0u, resolution 1.50Å

Drag the structure with the mouse to rotate

ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM

Overview

ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety of compounds across membranes of both prokaryotes and eukaryotes. The recently completed Escherichia coli genome sequence revealed that the largest family of paralogous E. coli proteins is composed of ABC transporters. Many eukaryotic proteins of medical significance belong to this family, such as the cystic fibrosis transmembrane conductance regulator (CFTR), the P-glycoprotein (or multidrug-resistance protein) and the heterodimeric transporter associated with antigen processing (Tap1-Tap2). Here we report the crystal structure at 1.5 A resolution of HisP, the ATP-binding subunit of the histidine permease, which is an ABC transporter from Salmonella typhimurium. We correlate the details of this structure with the biochemical, genetic and biophysical properties of the wild-type and several mutant HisP proteins. The structure provides a basis for understanding properties of ABC transporters and of defective CFTR proteins.

About this Structure

1B0U is a Single protein structure of sequence from Salmonella typhimurium with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ATP-binding subunit of an ABC transporter., Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH, Nature. 1998 Dec 17;396(6712):703-7. PMID:9872322

Page seeded by OCA on Thu Feb 21 11:50:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools