We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1e67

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e67.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1e67.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e67| PDB=1e67 | SCENE= }}
{{STRUCTURE_1e67| PDB=1e67 | SCENE= }}
-
'''ZN-AZURIN FROM PSEUDOMONAS AERUGINOSA'''
+
===ZN-AZURIN FROM PSEUDOMONAS AERUGINOSA===
-
==Overview==
+
<!--
-
Azurin*, a by-product of heterologous expression of the gene encoding the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli, was characterized by chemical analysis and electrospray ionization mass spectrometry, and its structure determined by X-ray crystallography. It was shown that azurin* is native azurin with its copper atom replaced by zinc in the metal binding site. Zinc is probably incorporated in the apo-protein after its expression and transport into the periplasm. Holo-azurin can be reconstituted from azurin* by prolonged exposure of the protein to high copper ion concentrations or unfolding of the protein and refolding in the presence of copper ions. An X-ray crystallographic analysis of azurin* at 0.21-nm resolution revealed that the overall structure of azurin is not perturbed by the metal exchange. However, the geometry of the co-ordination sphere changes from trigonal bipyramidal in the case of copper azurin to distorted tetrahedral for the zinc protein. The copper ligand Met121 is no longer co-ordinated to zinc which adopts a position close to the carbonyl oxygen atom from residue Gly45. The polypeptide structure surrounding the metal site undergoes moderate reorganization upon zinc binding. The largest displacement observed is for the carbonyl oxygen from residue Gly45, which is involved in copper and zinc binding. It moves by 0.03 nm towards the zinc, thereby reducing its distance to the metal from 0.29 nm in the copper protein to 0.23 nm in the derivative.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1576995}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1576995 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1576995}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt, A.]]
[[Category: Nar, H.]]
[[Category: Nar, H.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:13:05 2008''

Revision as of 21:13, 30 June 2008

Image:1e67.png

Template:STRUCTURE 1e67

ZN-AZURIN FROM PSEUDOMONAS AERUGINOSA

Template:ABSTRACT PUBMED 1576995

About this Structure

1E67 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin., Nar H, Huber R, Messerschmidt A, Filippou AC, Barth M, Jaquinod M, van de Kamp M, Canters GW, Eur J Biochem. 1992 May 1;205(3):1123-9. PMID:1576995

Page seeded by OCA on Tue Jul 1 00:13:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e67"
Personal tools