1mwy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1mwy.jpg|left|200px]]
{{Seed}}
[[Image:1mwy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mwy|  PDB=1mwy  |  SCENE=  }}  
{{STRUCTURE_1mwy|  PDB=1mwy  |  SCENE=  }}  


'''Solution structure of the N-terminal domain of ZntA in the apo-form'''
===Solution structure of the N-terminal domain of ZntA in the apo-form===




==Overview==
<!--
Zinc, a metal ion that functions in a wide variety of catalytic and structural sites in metalloproteins, is shown here to adopt a novel coordination environment in the Escherichia coli transport protein ZntA. The ZntA protein is a P-type ATPase that pumps zinc out of the cytoplasm and into the periplasm. It is physiologically selective for Zn(II) and functions with metalloregulatory proteins in the cell to keep the zinc quota within strict limits. Yet, the N-terminal cytoplasmic domain contains a region that is highly homologous to the yeast Cu(I) metallochaperone Atx1. To investigate how the structure of this region may influence its function, this fragment, containing residues 46-118, has been cloned out of the gene and overexpressed. We report here the solution structure of this fragment as determined by NMR. Both the apo and Zn(II)-ZntA(46-118) structures have been determined. It contains a previously unknown protein coordination site for zinc that includes two cysteine residues, Cys59 and Cys62, and a carboxylate residue, Asp58. The solvent accessibility of this site is also remarkably high, a feature that increasingly appears to be a characteristic of domains of heavy metal ion transport proteins. The participation of Asp58 in this ZntA metal ion binding site may play an important role in modulating the relative affinities and metal exchange rates for Zn(II)/Pb(II)/Cd(II) as compared with other P-type ATPases, which are selective for Cu(I) or Ag(I).
The line below this paragraph, {{ABSTRACT_PUBMED_12417201}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12417201 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12417201}}


==About this Structure==
==About this Structure==
1MWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWY OCA].  
1MWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWY OCA].  


==Reference==
==Reference==
Line 30: Line 34:
[[Category: Beta-alpha-beta-beta-alpha-beta]]
[[Category: Beta-alpha-beta-beta-alpha-beta]]
[[Category: Open-faced beta-sandwich fold]]
[[Category: Open-faced beta-sandwich fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:49:15 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:47:06 2008''

Revision as of 04:47, 29 July 2008

File:1mwy.png

Template:STRUCTURE 1mwy

Solution structure of the N-terminal domain of ZntA in the apo-form

Template:ABSTRACT PUBMED 12417201

About this Structure

1MWY is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)., Banci L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV, J Mol Biol. 2002 Nov 8;323(5):883-97. PMID:12417201

Page seeded by OCA on Tue Jul 29 07:47:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1mwy&oldid=733375"