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2vl1
From Proteopedia
(Difference between revisions)
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[[Image:2vl1.png|left|200px]] | [[Image:2vl1.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2vl1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lachancea_kluyveri Lachancea kluyveri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VL1 OCA]. | |
==Reference== | ==Reference== | ||
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[[Category: Di-zinc center]] | [[Category: Di-zinc center]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:38:02 2009'' | ||
Revision as of 00:19, 15 March 2011
CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE A GLY-GLY PEPTIDE
Template:ABSTRACT PUBMED 18448119
About this Structure
2vl1 is a 4 chain structure with sequence from Lachancea kluyveri. Full crystallographic information is available from OCA.
Reference
- Andersen B, Lundgren S, Dobritzsch D, Piskur J. A recruited protease is involved in catabolism of pyrimidines. J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:18448119 doi:10.1016/j.jmb.2008.03.073
- Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D. Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases. J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:14534321 doi:http://dx.doi.org/10.1074/jbc.M308674200
- Dobritzsch D, Gojkovic Z, Andersen B, Piskur J. Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:12832781
- Lundgren S, Andersen B, Piskur J, Dobritzsch D. Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements. J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:17916556 doi:http://dx.doi.org/10.1074/jbc.M705517200
