2hu9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2hu9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hu9, resolution 1.780&Aring;" /> '''X-ray structure of ...)
Line 4: Line 4:
==Overview==
==Overview==
-
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are, homologous to the human Wilson and Menkes disease proteins. The genome of, the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper, chaperone that contains an unusual cysteine-rich N-terminal domain of 130, amino acids in addition to a C-terminal copper binding domain with a, conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to, proteins found only in extremophiles and is the only such protein that is, fused to a copper chaperone. Surprisingly, optical, electron paramagnetic, resonance, and x-ray absorption spectroscopic data indicate the presence, of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper, ions, one in each domain. The 1.8 A resolution crystal structure of, CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold, and that the protein also binds a zinc ion at a four-cysteine site. CopZ, can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain, and is capable of reducing Cu2+ to Cu+. This unique fusion of a, redox-active domain with a CXXC-containing copper chaperone domain is, relevant to the evolution of copper homeostatic mechanisms and suggests, new models for copper trafficking.
+
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are homologous to the human Wilson and Menkes disease proteins. The genome of the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper chaperone that contains an unusual cysteine-rich N-terminal domain of 130 amino acids in addition to a C-terminal copper binding domain with a conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to proteins found only in extremophiles and is the only such protein that is fused to a copper chaperone. Surprisingly, optical, electron paramagnetic resonance, and x-ray absorption spectroscopic data indicate the presence of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper ions, one in each domain. The 1.8 A resolution crystal structure of CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold and that the protein also binds a zinc ion at a four-cysteine site. CopZ can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain and is capable of reducing Cu2+ to Cu+. This unique fusion of a redox-active domain with a CXXC-containing copper chaperone domain is relevant to the evolution of copper homeostatic mechanisms and suggests new models for copper trafficking.
==About this Structure==
==About this Structure==
Line 13: Line 13:
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Arguello, J.M.]]
+
[[Category: Arguello, J M.]]
[[Category: LeMoine, B.]]
[[Category: LeMoine, B.]]
-
[[Category: Rosenzweig, A.C.]]
+
[[Category: Rosenzweig, A C.]]
-
[[Category: Sazinsky, M.H.]]
+
[[Category: Sazinsky, M H.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: FES]]
[[Category: FES]]
Line 27: Line 27:
[[Category: metal transport]]
[[Category: metal transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:48:54 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:49 2008''

Revision as of 15:45, 21 February 2008

Image:2hu9.jpg

2hu9, resolution 1.780Å

Drag the structure with the mouse to rotate

X-ray structure of the Archaeoglobus fulgidus CopZ N-terminal Domain

Overview

Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are homologous to the human Wilson and Menkes disease proteins. The genome of the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper chaperone that contains an unusual cysteine-rich N-terminal domain of 130 amino acids in addition to a C-terminal copper binding domain with a conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to proteins found only in extremophiles and is the only such protein that is fused to a copper chaperone. Surprisingly, optical, electron paramagnetic resonance, and x-ray absorption spectroscopic data indicate the presence of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper ions, one in each domain. The 1.8 A resolution crystal structure of CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold and that the protein also binds a zinc ion at a four-cysteine site. CopZ can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain and is capable of reducing Cu2+ to Cu+. This unique fusion of a redox-active domain with a CXXC-containing copper chaperone domain is relevant to the evolution of copper homeostatic mechanisms and suggests new models for copper trafficking.

About this Structure

2HU9 is a Single protein structure of sequence from Archaeoglobus fulgidus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus., Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC, J Biol Chem. 2007 Aug 31;282(35):25950-9. Epub 2007 Jul 3. PMID:17609202

Page seeded by OCA on Thu Feb 21 17:45:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hu9"
Personal tools