3onf: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:3onf. | [[Image:3onf.png|left|200px]] | ||
<!-- | <!-- | ||
| Line 13: | Line 13: | ||
<!-- | <!-- | ||
The line below this paragraph, {{ | The line below this paragraph, {{ABSTRACT_PUBMED_22349223}}, adds the Publication Abstract to the page | ||
(as it appears on PubMed at http://www.pubmed.gov), where | (as it appears on PubMed at http://www.pubmed.gov), where 22349223 is the PubMed ID number. | ||
--> | --> | ||
{{ | {{ABSTRACT_PUBMED_22349223}} | ||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 22: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:018607106</ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references group="xtra"/> | <ref group="xtra">PMID:022349223</ref><ref group="xtra">PMID:018607106</ref><ref group="xtra">PMID:011732617</ref><ref group="xtra">PMID:009586999</ref><ref group="xtra">PMID:010387078</ref><ref group="xtra">PMID:015476817</ref><ref group="xtra">PMID:018815415</ref><ref group="xtra">PMID:015579379</ref><references group="xtra"/> | ||
[[Category: Adenosylhomocysteinase]] | [[Category: Adenosylhomocysteinase]] | ||
[[Category: Lupinus luteus]] | [[Category: Lupinus luteus]] | ||
Revision as of 08:26, 4 April 2012
Crystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepinCrystal structure of Lupinus luteus S-adenosyl-L-homocysteine hydrolase in complex with cordycepin
Template:ABSTRACT PUBMED 22349223
About this StructureAbout this Structure
3onf is a 2 chain structure with sequence from Lupinus luteus. Full crystallographic information is available from OCA.
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5][xtra 6][xtra 7][xtra 8]
- ↑ Brzezinski K, Dauter Z, Jaskolski M. High-resolution structures of complexes of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus). Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):218-31. Epub 2012 Feb 7. PMID:22349223 doi:10.1107/S0907444911055090
- ↑ Brzezinski K, Bujacz G, Jaskolski M. Purification, crystallization and preliminary crystallographic studies of plant S-adenosyl-L-homocysteine hydrolase (Lupinus luteus). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt, 7):671-3. Epub 2008 Jun 28. PMID:18607106 doi:10.1107/S1744309108017703
- ↑ Brzezinski K, Janowski R, Podkowinski J, Jaskolski M. Sequence determination and analysis of S-adenosyl-L-homocysteine hydrolase from yellow lupine (Lupinus luteus). Acta Biochim Pol. 2001;48(2):477-83. PMID:11732617
- ↑ Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL. Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol. 1998 May;5(5):369-76. PMID:9586999
- ↑ Hu Y, Komoto J, Huang Y, Gomi T, Ogawa H, Takata Y, Fujioka M, Takusagawa F. Crystal structure of S-adenosylhomocysteine hydrolase from rat liver. Biochemistry. 1999 Jun 29;38(26):8323-33. PMID:10387078 doi:10.1021/bi990332k
- ↑ Tanaka N, Nakanishi M, Kusakabe Y, Shiraiwa K, Yabe S, Ito Y, Kitade Y, Nakamura KT. Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum. J Mol Biol. 2004 Oct 29;343(4):1007-17. PMID:15476817 doi:10.1016/j.jmb.2004.08.104
- ↑ Reddy MC, Kuppan G, Shetty ND, Owen JL, Ioerger TR, Sacchettini JC. Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with substrate and inhibitors. Protein Sci. 2008 Dec;17(12):2134-44. Epub 2008 Sep 24. PMID:18815415 doi:10.1110/ps.038125.108
- ↑ Stepkowski T, Brzezinski K, Legocki AB, Jaskolski M, Bena G. Bayesian phylogenetic analysis reveals two-domain topology of S-adenosylhomocysteine hydrolase protein sequences. Mol Phylogenet Evol. 2005 Jan;34(1):15-28. PMID:15579379 doi:10.1016/j.ympev.2004.09.008