1uzh: Difference between revisions

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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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==About this Structure==
==About this Structure==
1UZH is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/ ]] with MG, CAP and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UZH OCA]].  
1UZH is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii,_synechococcus_sp Chlamydomonas reinhardtii, synechococcus sp]] and [[http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]] with MG, CAP and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UZH OCA]].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16026157 16026157]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16026157 16026157]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii, synechococcus sp]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Andersson, I.]]
[[Category: Andersson, I.]]
[[Category: Karkehabadi, S.]]
[[Category: Karkehabadi, S.]]
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[[Category: transit peptide]]
[[Category: transit peptide]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:47:33 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:21:57 2007''

Revision as of 12:17, 30 October 2007

File:1uzh.gif


1uzh, resolution 2.20Å

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A CHIMERIC CHLAMYDOMONAS, SYNECHOCOCCUS RUBISCO ENZYME

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 [Chlamydomonas reinhardtii, synechococcus sp] and [Chlamydomonas reinhardtii] with MG, CAP and EDO as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Site: AC1. 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

Page seeded by OCA on Tue Oct 30 11:21:57 2007

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