2fta: Difference between revisions

Revision as of 23:26, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fta.png

Template:STRUCTURE 2fta

Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"

Template:ABSTRACT PUBMED 16651527

About this StructureAbout this Structure

2FTA is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin., Li C, Yanagisawa S, Martins BM, Messerschmidt A, Banfield MJ, Dennison C, Proc Natl Acad Sci U S A. 2006 May 9;103(19):7258-63. Epub 2006 May 1. PMID:16651527

Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip., Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW, J Mol Biol. 1991 Oct 5;221(3):765-72. PMID:1942029

Loop-contraction mutagenesis of type 1 copper sites., Yanagisawa S, Dennison C, J Am Chem Soc. 2004 Dec 8;126(48):15711-9. PMID:15571393

Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus., Romero A, Nar H, Huber R, Messerschmidt A, Kalverda AP, Canters GW, Durley R, Mathews FS, J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:8120896

Page seeded by OCA on Sun Jul 27 23:26:05 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2fta.gif|left|200px]]
+{{Seed}}
+[[Image:2fta.png|left|200px]]
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 {{STRUCTURE_2fta|  PDB=2fta  |  SCENE=  }}
-'''Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"'''
+===Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"===
-==Overview==
+<!--
-The main active-site loop of the copper-binding protein azurin (a cupredoxin) has been shortened from C(112)TFPGH(117)SALM(121) to C(112)TPH(115)PFM(118) (the native loop from the cupredoxin amicyanin) and also to C(112)TPH(115)PM(117). The Cu(II) site structure is almost unaffected by shortening, as is that of the Cu(I) center at alkaline pH in the variant with the C(112)TPH(115)PM(117) loop sequence. Subtle spectroscopic differences due to alterations in the spin density distribution at the Cu(II) site can be attributed mainly to changes in the hydrogen-bonding pattern. Electron transfer is almost unaffected by the introduction of the C(112)TPH(115)PFM(118) loop, but removal of the Phe residue has a sizable effect on reactivity, probably because of diminished homodimer formation. At mildly acidic pH values, the His-115 ligand protonates and dissociates from the cuprous ion, an effect that has a dramatic influence on the reactivity of cupredoxins. These studies demonstrate that the amicyanin loop adopts a conformation identical to that found in the native protein when introduced into azurin, that a shorter than naturally occurring C-terminal active-site loop can support a functional T1 copper site, that CTPHPM is the minimal loop length required for binding this ubiquitous electron transfer center, and that the length and sequence of a metal-binding loop regulates a range of structural and functional features of the active site of a metalloprotein.
+The line below this paragraph, {{ABSTRACT_PUBMED_16651527}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16651527 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16651527}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin., Li C, Yanagisawa S, Martins BM, Messerschmidt A, Banfield MJ, Dennison C, Proc Natl Acad Sci U S A. 2006 May 9;103(19):7258-63. Epub 2006 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16651527 16651527]
+Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip., Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW, J Mol Biol. 1991 Oct 5;221(3):765-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1942029 1942029]
+Loop-contraction mutagenesis of type 1 copper sites., Yanagisawa S, Dennison C, J Am Chem Soc. 2004 Dec 8;126(48):15711-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571393 15571393]
+Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus., Romero A, Nar H, Huber R, Messerschmidt A, Kalverda AP, Canters GW, Durley R, Mathews FS, J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8120896 8120896]
 [[Category: Pseudomonas aeruginosa]]
 [[Category: Single protein]]
@@ Line 25: / Line 35: @@
 [[Category: Blue copper-binding protein]]
 [[Category: Greek-key beta-barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:17:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:26:05 2008''