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2hx8

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{{STRUCTURE_2hx8| PDB=2hx8 | SCENE= }}
{{STRUCTURE_2hx8| PDB=2hx8 | SCENE= }}
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'''Crystal structure of Cu(I) Azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CSPHQGAGM", at pH5'''
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===Crystal structure of Cu(I) Azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CSPHQGAGM", at pH5===
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==Overview==
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The ligand-containing loops of two copper-binding electron-transfer proteins (cupredoxins) have been swapped. In the azurin (AZ) variant in which the plastocyanin (PC) sequence is introduced (AZPC), the loop adopts a conformation identical to that in PC. The reduction potential of AZPC is raised as compared to AZ and matches that of PC. In the previously published AZAMI variant (AMI = amicyanin), the shorter introduced loop adopts the same conformation as in AMI, and the reduction potential is lowered to equal that of AMI (Yanagisawa, S.; Dennison, C. J. Am. Chem. Soc. 2004, 126, 15711-15719. Li, C.; et al. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 7258-7263). Thus, the loop structure plays an important role in tuning the reduction potential of a type 1 copper site with contributions from protein dipoles in this region probably the most important feature. The structure of the loop also seems to be a major factor in controlling dissociation and protonation of the C-terminal His ligand, which can act as a switch to regulate electron-transfer reactivity. The PCAZ variant (PC with the AZ loop) possesses an active site, which is different from those of both PC and AZ, and it is assumed that the introduced loop does not adopt a structure as in AZ. This contributes to the observed instability of PCAZ and highlights that loop-scaffold interactions are important for stabilizing the active site of a cupredoxin.
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(as it appears on PubMed at http://www.pubmed.gov), where 17227035 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17227035}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins., Li C, Banfield MJ, Dennison C, J Am Chem Soc. 2007 Jan 24;129(3):709-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17227035 17227035]
Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins., Li C, Banfield MJ, Dennison C, J Am Chem Soc. 2007 Jan 24;129(3):709-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17227035 17227035]
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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]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Greek-key beta-barrel]]
[[Category: Greek-key beta-barrel]]
[[Category: Loop mutagenesis]]
[[Category: Loop mutagenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:49:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:42:06 2008''

Revision as of 20:42, 28 July 2008

Image:2hx8.png

Template:STRUCTURE 2hx8

Crystal structure of Cu(I) Azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CSPHQGAGM", at pH5

Template:ABSTRACT PUBMED 17227035

About this Structure

2HX8 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins., Li C, Banfield MJ, Dennison C, J Am Chem Soc. 2007 Jan 24;129(3):709-18. PMID:17227035

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

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