2ga7: Difference between revisions

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Revision as of 03:13, 31 March 2008

File:2ga7.gif

Ligands:

Gene:

ATP7A, MC1, MNK (Homo sapiens)

Activity:

Copper-exporting ATPase, with EC number 3.6.3.4

Related:

2G9O

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)

OverviewOverview

The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3 is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded beta-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains.

About this StructureAbout this Structure

2GA7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein., Banci L, Bertini I, Cantini F, DellaMalva N, Herrmann T, Rosato A, Wuthrich K, J Biol Chem. 2006 Sep 29;281(39):29141-7. Epub 2006 Jul 26. PMID:16873374

Page seeded by OCA on Mon Mar 31 03:13:54 2008

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OCA

@@ Line 4: / Line 4: @@
 |PDB= 2ga7 |SIZE=350|CAPTION= <scene name='initialview01'>2ga7</scene>
 |SITE=
-|LIGAND= <scene name='pdbligand=CU1:COPPER (I) ION'>CU1</scene>
+|LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4]
+|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </span>
 |GENE= ATP7A, MC1, MNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+|DOMAIN=
+|RELATEDENTRY=[[2g9o|2G9O]]
+|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ga7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ga7 OCA], [http://www.ebi.ac.uk/pdbsum/2ga7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ga7 RCSB]</span>
 }}
@@ Line 14: / Line 17: @@
 ==Overview==
 The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3 is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded beta-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains.
-==Disease==
-Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific , OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Cutis laxa, neonatal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Melanoma susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Menkes disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Occipital horn syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Oculocutaneous albinism, type II, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Skin/hair/eye pigmentation 2, blond hair/fair skin OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Skin/hair/eye pigmentation 2, red hair/fair skin OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], UV-induced skin damage OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]]
 ==About this Structure==
@@ Line 34: / Line 34: @@
 [[Category: SPINE, Structural Proteomics in Europe.]]
 [[Category: Wuthrich, K.]]
-[[Category: CU1]]
 [[Category: copper(i)]]
 [[Category: menkes disease-associated protein]]
@@ Line 43: / Line 42: @@
 [[Category: structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:02:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:13:54 2008''