1waz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1waz.gif|left|200px]]<br /><applet load="1waz" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1waz.gif|left|200px]]
-
caption="1waz" />
+
 
-
'''NMR STRUCTURE DETERMINATION OF THE BACTERIAL MERCURY TRANSPORTER, MERF, IN MICELLES'''<br />
+
{{Structure
 +
|PDB= 1waz |SIZE=350|CAPTION= <scene name='initialview01'>1waz</scene>
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''NMR STRUCTURE DETERMINATION OF THE BACTERIAL MERCURY TRANSPORTER, MERF, IN MICELLES'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1WAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Morganella_morganii Morganella morganii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAZ OCA].
+
1WAZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Morganella_morganii Morganella morganii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAZ OCA].
==Reference==
==Reference==
-
NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system., Howell SC, Mesleh MF, Opella SJ, Biochemistry. 2005 Apr 5;44(13):5196-206. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15794657 15794657]
+
NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system., Howell SC, Mesleh MF, Opella SJ, Biochemistry. 2005 Apr 5;44(13):5196-206. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15794657 15794657]
[[Category: Morganella morganii]]
[[Category: Morganella morganii]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 24: Line 33:
[[Category: transport protein]]
[[Category: transport protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:24 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:33 2008''

Revision as of 12:54, 20 March 2008


PDB ID 1waz

Drag the structure with the mouse to rotate
Coordinates: save as pdb, mmCIF, xml



NMR STRUCTURE DETERMINATION OF THE BACTERIAL MERCURY TRANSPORTER, MERF, IN MICELLES


Overview

The three-dimensional backbone structure of a membrane protein with two transmembrane helices in micelles was determined using solution NMR methods that rely on the measurement of backbone (1)H-(15)N residual dipolar couplings (RDCs) from samples of two different constructs that align differently in stressed polyacrylamide gels. Dipolar wave fitting to the (1)H-(15)N RDCs determines the helical boundaries based on periodicity and was utilized in the generation of supplemental dihedral restraints for the helical segments. The (1)H-(15)N RDCs and supplemental dihedral restraints enable the determination of the structure of the helix-loop-helix core domain of the mercury transport membrane protein MerF with a backbone RMSD of 0.58 A. Moreover, the fold of this polypeptide demonstrates that the two vicinal pairs of cysteine residues, shown to be involved in the transport of Hg(II) across the membrane, are exposed to the cytoplasm. This finding differs from earlier structural and mechanistic models that were based primarily on the somewhat atypical hydropathy plot for MerF and related transport proteins.

About this Structure

1WAZ is a Single protein structure of sequence from Morganella morganii. Full crystallographic information is available from OCA.

Reference

NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system., Howell SC, Mesleh MF, Opella SJ, Biochemistry. 2005 Apr 5;44(13):5196-206. PMID:15794657

Page seeded by OCA on Thu Mar 20 14:54:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools