1cuo
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(New page: 200px<br /><applet load="1cuo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cuo, resolution 1.60Å" /> '''CRYSTAL STRUCTURE AN...)
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Revision as of 10:39, 20 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J
Overview
The obligate methylotroph Methylomonas sp. strain J produces two azurins, (Az-iso1 and Az-iso2) as candidates for electron acceptor from methylamine, dehydrogenase (MADH) in the electron-transfer process involving the, oxidation of methylamine to formaldehyde and ammonia. The X-ray, crystallographic study indicated that Az-iso2 gives two types of crystals, (form I and form II) with polyethylene glycol (PEG4000) and ammonium, sulfate as the precipitants, respectively. Comparison between the two, Az-iso2 structures in forms I and II reveals the remarkable structural, changes at the top surface of the molecule around the copper atom. Az-iso2, possesses Gly43 instead of Val43 or Ala43, which is unique among all other, azurins around the copper ligand His46, inducing the remarkable structural, change in the loop region from Gly37 to Gly43. When the structure of, Az-iso2 is superimposed on that of amicyanin in the ternary complex, composed of MADH, amicyanin, and cytochrome c(551), the loop of Az-iso2, deeply overlaps with the light subunit of MADH. However, the Az-iso2, molecule is probably able to avoid any steric hindrance with the cognate, MADH to form the complex for intermolecular electron-transfer reaction, since the loop containing Gly43 is flexible. We discuss why the, electron-transfer activity of Az-iso2 is fivefold higher than that of, Az-iso1.
About this Structure
1CUO is a Single protein structure of sequence from Methylomonas sp. j with CU as ligand. Full crystallographic information is available from OCA.
Reference
The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J., Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y, J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:14516747
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