1afj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1afj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1afj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1afj| PDB=1afj | SCENE= }}
{{STRUCTURE_1afj| PDB=1afj | SCENE= }}
-
'''STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES'''
+
===STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES===
-
==Overview==
+
<!--
-
Bacteria carrying plasmids with the mer operon, which encodes the proteins responsible for the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell membrane into the cytoplasm where it is reduced to Hg(0). This is significant because metallic mercury is relatively nontoxic and volatile and thus can be passively eliminated. The structures of the reduced and mercury-bound forms of merP, the periplasmic protein, which binds Hg(II) and transfers it to the membrane transport protein merT, have been determined in aqueous solution by multidimensional NMR spectroscopy. The 72-residue merP protein has a betaalpha betabeta alphabeta fold with the two alpha helices overlaying a four-strand antiparallel beta sheet. Structural differences between the reduced and mercury-bound forms of merP are localized to the metal binding loop containing the consensus sequence GMTCXXC. The structure of the mercury-bound form of merP shows that Hg(II) is bicoordinate with the Cys side chain ligands, and this is confirmed by the chemical shift frequency of the 199Hg resonance.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9188683}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9188683 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9188683}}
==About this Structure==
==About this Structure==
-
1AFJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFJ OCA].
+
1AFJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFJ OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Mercury detoxification]]
[[Category: Mercury detoxification]]
[[Category: Periplasmic]]
[[Category: Periplasmic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:12:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:44:27 2008''

Revision as of 13:44, 30 June 2008

Image:1afj.png

Template:STRUCTURE 1afj

STRUCTURE OF THE MERCURY-BOUND FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9188683

About this Structure

1AFJ is a Single protein structure of sequence from Shigella flexneri. Full experimental information is available from OCA.

Reference

Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system., Steele RA, Opella SJ, Biochemistry. 1997 Jun 10;36(23):6885-95. PMID:9188683

Page seeded by OCA on Mon Jun 30 16:44:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1afj"
Personal tools