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Sökning: onr:"swepub:oai:DiVA.org:uu-63209" > First crystal struc...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00002447naa a2200325 4500
001oai:DiVA.org:uu-63209
003SwePub
008081017s2001 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-632092 URI
024a https://doi.org/10.1074/jbc.M1077652002 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Taylor, Thomas C4 aut
2451 0a First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii
264 1c 2001
338 a print2 rdacarrier
520 a The crystal structure of Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) from the unicellular green alga, Chlamydomonas reinhardtii has been determined to 1.4 Angstrom resolution. Overall, the structure shows high similarity to the previously determined structures of L8S8 Rubisco enzymes. The largest difference is found in the loop between beta strands A and B of the small subunit (betaA-betaB loop), which is longer by six amino acid residues than the corresponding region in Rubisco from Spinacia. Mutations of residues in the betaA-betaB loop have been shown to affect holoenzyme stability and catalytic properties. The information contained in the Chlamydomonas structure enables a more reliable analysis of the effect of these mutations. No electron density was observed for the last 13 residues of the small subunit, which are assumed to be disordered in the crystal. Because of the high resolution of the data, some posttranslational modifications are unambiguously apparent in the structure. These include cysteine and N-terminal methylations and proline 4-hydroxylations.
650 7a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng
700a Backlund, Andersu Uppsala universitet,Avdelningen för farmakognosi4 aut0 (Swepub:uu)andeback
700a Björhall, Karin4 aut
700a Spreitzer, Robert J.4 aut
700a Andersson, Inger4 aut
710a Uppsala universitetb Avdelningen för farmakognosi4 org
773t Journal of Biological Chemistryg 276:51, s. 48159-48164q 276:51<48159-48164x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-63209
8564 8u https://doi.org/10.1074/jbc.M107765200

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