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InterPro: IPR008972 Cupredoxin

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UniProtKB
Matches:
31817 proteins
AccessionHelp
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IPR008972 Cupredoxin
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Children IPR000923 Blue (type 1) copper domain
IPR002429 Cytochrome c oxidase subunit II C-terminal
IPR013732 Protein-arginine deiminase (PAD) N-terminal
Found in IPR001799 Ephrin
IPR006376 Copper-resistance protein CopA
IPR010532 Sulfocyanin
IPR012746 Nitrite reductase, copper containing
IPR014707 Coagulation factor VIII
IPR017527 Nitrosocyanin
IPR017760 L-ascorbate oxidase, plants
IPR017761 Laccase
IPR017762 L-ascorbate oxidase, fungi
Contains IPR001117 Multicopper oxidase, type 1
IPR001505 Copper centre Cu(A)
IPR002355 Multicopper oxidase, copper-binding site
IPR003245 Plastocyanin-like
IPR010514 COX aromatic rich
IPR011706 Multicopper oxidase, type 2
IPR011707 Multicopper oxidase, type 3
IPR019765 Ephrin, conserved site
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free copper is toxic, even at very low concentrations, its homeostasis in living organisms is tightly controlled by subtle molecular mechanisms. In eukaryotes, before being transported inside the cell via the high-affinity copper transporters of the CTR family, the copper (II) ion is reduced to copper (I). In blue copper proteins such as Cupredoxin, the copper (I) ion form is stabilised by a constrained His2Cys coordination environment.

This entry represents cupredoxin proteins, as well as structural homologues to cupredoxin. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel [1]. Some of these proteins have lost the ability to bind copper. Proteins with a cupredoxin-type fold are found in the following family groups:

  • Mono-domain cupredoxins, such as amicyanin, plastocyanin, pseudoazurin, plantacyanin, azurin, auracyanin, rusticyanin, stellacyanin, and mavicyanin.
  • Multi-domain cupredoxins, such as nitrite reductase (2 domains of this fold), multicopper oxidase CueO, spore coat protein A, ascorbate oxidase (3 domains of this fold), laccase (3 domains of this fold), ceruloplamin (6 domains of this fold), and coagulation factor V.
  • Red copper protein nitrocyanin and the C-terminal of nitrous oxide reductase.
  • Quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II.
  • Ephrin-a5 and ephrin-b2 ectodomain, which are related to cupredoxins but lack the metal-binding site.
  • The N-terminal domain of protein arginine deiminase Pad4, which is related to cupredoxin but lacks the metal-biding site.
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1a3z , 1a4a , 1a4b , 1a4c , 1a65 , 1a8z , 1aac , 1aaj , 1aan , 1adw , 1ag0 , 1ag6 , 1aiz , 1aoz , 1aq8 , 1ar1 , 1as6 , 1as7 , 1as8 , 1aso , 1asp , 1asq , 1azb , 1azc , 1azn , 1azr , 1azu , 1b3i , 1baw , 1bex , 1bq5 , 1bqk , 1bqr , 1bxa , 1bxu , 1bxv , 1byo , 1byp , 1cc3 , 1cuo , 1cur , 1cyw , 1cyx , 1dyz , 1dz0 , 1e30 , 1e5y , 1e5z , 1e65 , 1e67 , 1ehk , 1et5 , 1et7 , 1et8 , 1etj , 1ezl , 1f56 , 1fa4 , 1fft , 1fwx , 1gr7 , 1gs6 , 1gs7 , 1gs8 , 1gsk , 1gw0 , 1gy1 , 1gy2 , 1gyc , 1hau , 1haw , 1hfu , 1i53 , 1iby , 1ibz , 1ic0 , 1id2 , 1iko , 1ils , 1ilu , 1iuz , 1j5c , 1j5d , 1j9q , 1j9r , 1j9s , 1j9t , 1jer , 1joi , 1jvl , 1jvo , 1jxd , 1jxf , 1jxg , 1jze , 1jzf , 1jzg , 1jzh , 1jzi , 1jzj , 1kbv , 1kbw , 1kcb , 1kcw , 1kdi , 1kdj , 1kgy , 1kv7 , 1kya , 1l9o , 1l9p , 1l9q , 1l9r , 1l9s , 1l9t , 1m56 , 1m57 , 1m9w , 1mda , 1mg2 , 1mg3 , 1mzy , 1mzz , 1n68 , 1n70 , 1ndr , 1nds , 1ndt , 1nia , 1nib , 1nic , 1nid , 1nie , 1nif , 1nin , 1npj , 1npn , 1ntd , 1nwo , 1nwp , 1nzr , 1occ , 1oco , 1ocr , 1ocz , 1oe1 , 1oe2 , 1oe3 , 1of0 , 1oow , 1ov8 , 1paz , 1pcs , 1pf3 , 1pla , 1plb , 1plc , 1pmy , 1pnc , 1pnd , 1py0 , 1pza , 1pzb , 1pzc , 1qhq , 1qle , 1qni , 1r1c , 1rcy , 1rkr , 1rzp , 1rzq , 1sdd , 1sf3 , 1sf5 , 1sfd , 1sfh , 1shw , 1shx , 1sjm , 1snr , 1t5k , 1tef , 1teg , 1tkw , 1tu2 , 1uat , 1uri , 1uvw , 1v10 , 1v54 , 1v55 , 1vlx , 1w6l , 1w6w , 1w8e , 1wa0 , 1wa1 , 1wa2 , 1wae , 1wd8 , 1wd9 , 1wda , 1ws7 , 1ws8 , 1x9r , 1x9u , 1xb3 , 1xb6 , 1xb8 , 1xme , 1ylb , 1zdq , 1zds , 1zia , 1zib , 1zv2 , 2a3t , 2aan , 2afn , 2avf , 2aza , 2azu , 2b08 , 2b3i , 2bhf , 2bo0 , 2bp0 , 2bp8 , 2bw4 , 2bw5 , 2bwd , 2bwi , 2bz7 , 2bzc , 2cak , 2cal , 2cbp , 2ccw , 2cj3 , 2cua , 2dew , 2dex , 2dey , 2dw5 , 2dws , 2dwt , 2dy2 , 2dyr , 2dys , 2e86 , 2eij , 2eik , 2eil , 2eim , 2ein , 2fjs , 2fnw , 2fqd , 2fqe , 2fqf , 2fqg , 2ft6 , 2ft7 , 2ft8 , 2fta , 2fwl , 2gb2 , 2gba , 2gc4 , 2gc7 , 2ghz , 2gi0 , 2gim , 2gsm , 2h3x , 2h47 , 2hle , 2hrg , 2hrh , 2hx7 , 2hx8 , 2hx9 , 2hxa , 2hzh , 2i7o , 2i7s , 2iaa , 2idf , 2idq , 2ids , 2idt , 2idu , 2ih8 , 2ih9 , 2iwe , 2iwf , 2iwk , 2j55 , 2j56 , 2j57 , 2j5w , 2jfc , 2jxm , 2mta , 2nrd , 2occ , 2oj1 , 2ov0 , 2p80 , 2pcf , 2pcy , 2plt , 2pp7 , 2pp8 , 2pp9 , 2ppa , 2ppc , 2ppd , 2ppe , 2ppf , 2q5b , 2q9o , 2qdv , 2qdw , 2qpd , 2qpe , 2qt6 , 2rac , 2tsa , 2tsb , 2ux6 , 2ux7 , 2uxf , 2uxg , 2vm3 , 2vm4 , 2vw4 , 2vw6 , 2vw7 , 3azu , 3bvd , 3dtu , 3ehb , 3paz , 3pcy , 4azu , 4paz , 4pcy , 5azu , 5paz , 5pcy , 6paz , 6pcy , 7paz , 7pcy , 8paz , 9pcy

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR008972 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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O08543 Ephrin-A5

O43921 Ephrin-A2

O44516 Ephrin-4

P00408 Cytochrome c oxidase subunit 2

P38993 Iron transport multicopper oxidase FET3

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR019765 Ephrin, conserved site
IPR002355 Multicopper oxidase, copper-binding site
IPR011759 Cytochrome C oxidase subunit II, transmembrane domain
IPR014222 Cytochrome c oxidase, subunit II
IPR011706 Multicopper oxidase, type 2
IPR011707 Multicopper oxidase, type 3
IPR001117 Multicopper oxidase, type 1
IPR015964 Cytochrome C oxidase subunit II-like, transmembrane domain
IPR002429 Cytochrome c oxidase subunit II C-terminal
IPR001505 Copper centre Cu(A)
IPR001799 Ephrin
IPR008972 Cupredoxin
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
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1. Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR.
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A. 99 2766-71 2002 [PubMed: 11867755]
http://dx.doi.org/10.1073/pnas.052710499

Additional ReadingHelp
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Tocheva EI, Eltis LD, Murphy ME.
Conserved active site residues limit inhibition of a copper-containing nitrite reductase by small molecules.
Biochemistry 47 2008 4452-60 [PubMed: 18358002]
http://dx.doi.org/10.1021/bi7020537
Hulsker R, Baranova MV, Bullerjahn GS, Ubbink M.
Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica.
J. Am. Chem. Soc. 130 2008 1985-91 [PubMed: 18201089]
http://dx.doi.org/10.1021/ja077453p
Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB.
Tryptophan-accelerated electron flow through proteins.
Science 320 2008 1760-2 [PubMed: 18583608]
http://dx.doi.org/10.1126/science.1158241
Hough MA, Antonyuk SV, Strange RW, Eady RR, Hasnain SS.
Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase.
J. Mol. Biol. 378 2008 353-61 [PubMed: 18353369]
http://dx.doi.org/10.1016/j.jmb.2008.01.097
Hakulinen N, Andberg M, Kallio J, Koivula A, Kruus K, Rouvinen J.
A near atomic resolution structure of a Melanocarpus albomyces laccase.
J. Struct. Biol. 162 2008 29-39 [PubMed: 18249560]
http://dx.doi.org/10.1016/j.jsb.2007.12.003
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InterPro 23.1