This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2hq3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hq3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hq3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hq3| PDB=2hq3 | SCENE= }}
{{STRUCTURE_2hq3| PDB=2hq3 | SCENE= }}
-
'''Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes'''
+
===Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes===
-
==Overview==
+
<!--
-
The formation of the unique catalytic tetranuclear copper cluster (Cu(Z)) of nitrous oxide reductase, N(2)OR, requires the coexpression of a multiprotein assembly apparatus encoded by the nosDFYL operon. NosL, one of the proteins encoded by this transcript, is a 20 kDa lipoprotein of the periplasm that has been shown to bind copper(I), although its function has yet to be detemined. Cu(I) EXAFS data collected on the holo protein demonstrated that features of the copper binding site are consistent with a role for this protein as a metallochaperone, a class of metal ion transporters involved in metal resistance, homeostasis, and metallocluster biosynthesis. To test this hypothesis and to gain insight into other potential functional roles for this protein in the N(2)OR system, the three-dimensional solution structure of apo NosL has been solved by solution NMR methods. The structure of apo NosL consists of two relatively independent homologous domains that adopt an unusual betabetaalphabeta topology. The fold of apo NosL displays structural homology to only one other protein, MerB, an organomercury lyase involved in bacterial mercury resistance (Di Lello et al. (2004) Biochemistry 43, 8322-32). The structural similarity between apo NosL and MerB, together with the absolute conservation of Met109 in all NosL sequences, indicates that this residue may be involved in copper ligation, and that the metal binding site is likely to be solvent-accessible and contiguous with a large binding cleft. The structural observations suggest that NosL is exceptionally adapted for a role in copper and/or sulfur delivery and possibly for metallochaperone function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17014077}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17014077 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17014077}}
==About this Structure==
==About this Structure==
-
2HQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQ3 OCA].
+
2HQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQ3 OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Taubner, L M.]]
[[Category: Taubner, L M.]]
[[Category: Alpha beta topology]]
[[Category: Alpha beta topology]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:34:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:50:51 2008''

Revision as of 05:50, 28 July 2008

Image:2hq3.png

Template:STRUCTURE 2hq3

Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes

Template:ABSTRACT PUBMED 17014077

About this Structure

2HQ3 is a Single protein structure of sequence from Achromobacter cycloclastes. Full experimental information is available from OCA.

Reference

Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein., Taubner LM, McGuirl MA, Dooley DM, Copie V, Biochemistry. 2006 Oct 10;45(40):12240-52. PMID:17014077

Page seeded by OCA on Mon Jul 28 08:50:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hq3"
Personal tools