1uzh

Revision as of 18:42, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1uzh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uzh, resolution 2.20Å" /> '''A CHIMERIC CHLAMYDO...)
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A CHIMERIC CHLAMYDOMONAS, SYNECHOCOCCUS RUBISCO ENZYME

File:1uzh.gif


1uzh, resolution 2.20Å

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OverviewOverview

Comparison of subunit sequences and X-ray crystal structures of, ribulose-1,5-bisphosphate carboxylase/oxygenase indicates that the loop, between beta-strands A and B of the small subunit is one of the most, variable regions of the holoenzyme. In prokaryotes and nongreen algae, the, loop contains 10 residues. In land plants and green algae, the loop is, comprised of approximately 22 and 28 residues, respectively. Previous, studies indicated that the longer betaA-betaB loop was required for the, assembly of cyanobacterial small subunits with plant large subunits in, isolated chloroplasts. In the present study, chimeric small subunits were, constructed by replacing the loop of the green alga Chlamydomonas, reinhardtii with the sequences of Synechococcus or spinach. When these, engineered ... [(full description)]

About this StructureAbout this Structure

1UZH is a [Protein complex] structure of sequences from [[1]] with MG, CAP and EDO as [ligands]. Active as [[2]], with EC number [4.1.1.39]. Full crystallographic information is available from [OCA].

ReferenceReference

Chimeric small subunits influence catalysis without causing global conformational changes in the crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase., Karkehabadi S, Peddi SR, Anwaruzzaman M, Taylor TC, Cederlund A, Genkov T, Andersson I, Spreitzer RJ, Biochemistry. 2005 Jul 26;44(29):9851-61. PMID:16026157

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