1q44
From Proteopedia
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{{STRUCTURE_1q44| PDB=1q44 | SCENE= }} | {{STRUCTURE_1q44| PDB=1q44 | SCENE= }} | ||
| + | ===Crystal Structure of an Arabidopsis Thaliana Putative Steroid Sulfotransferase=== | ||
| - | == | + | ==Function== |
| - | + | [[http://www.uniprot.org/uniprot/FSTL_ARATH FSTL_ARATH]] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the stereospecific sulfate conjugation of 24-epibrassinosteroids. Preferred substrates are 24-epicathasterone and 6-deoxo-24-epicathasterone. Low activity with 22-deoxy-24-epiteasterone. No activity with 24-epimers catasterone and brassinolide. Sulfonates salicylic acid. May be involved in detoxification. Enhances plant response to pathogen infection and contributes to long distance signaling in systemic acquired resistance (SAR).<ref>PMID:17039368</ref> <ref>PMID:20374532</ref> | |
==About this Structure== | ==About this Structure== | ||
| - | + | [[1q44]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q44 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015317023</ref><references group="xtra"/><references/> |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Bingman, C A.]] | [[Category: Bingman, C A.]] | ||
[[Category: CESG, Center for Eukaryotic Structural Genomics.]] | [[Category: CESG, Center for Eukaryotic Structural Genomics.]] | ||
[[Category: Johnson, K A.]] | [[Category: Johnson, K A.]] | ||
| - | [[Category: | + | [[Category: Phillips, G N.]] |
[[Category: Smith, D W.]] | [[Category: Smith, D W.]] | ||
[[Category: Apo]] | [[Category: Apo]] | ||
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[[Category: Cesg]] | [[Category: Cesg]] | ||
[[Category: Protein structure initiative]] | [[Category: Protein structure initiative]] | ||
| - | [[Category: Steroid | + | [[Category: Steroid sulfotransferase]] |
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
| - | + | [[Category: Transferase]] | |
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Revision as of 10:41, 16 April 2014
Contents |
Crystal Structure of an Arabidopsis Thaliana Putative Steroid Sulfotransferase
Function
[FSTL_ARATH] Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the stereospecific sulfate conjugation of 24-epibrassinosteroids. Preferred substrates are 24-epicathasterone and 6-deoxo-24-epicathasterone. Low activity with 22-deoxy-24-epiteasterone. No activity with 24-epimers catasterone and brassinolide. Sulfonates salicylic acid. May be involved in detoxification. Enhances plant response to pathogen infection and contributes to long distance signaling in systemic acquired resistance (SAR).[1] [2]
About this Structure
1q44 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
- Smith DW, Johnson KA, Bingman CA, Aceti DJ, Blommel PG, Wrobel RL, Frederick RO, Zhao Q, Sreenath H, Fox BG, Volkman BF, Jeon WB, Newman CS, Ulrich EL, Hegeman AD, Kimball T, Thao S, Sussman MR, Markley JL, Phillips GN Jr. Crystal structure of At2g03760, a putative steroid sulfotransferase from Arabidopsis thaliana. Proteins. 2004 Dec 1;57(4):854-7. PMID:15317023 doi:10.1002/prot.20258
- ↑ Marsolais F, Boyd J, Paredes Y, Schinas AM, Garcia M, Elzein S, Varin L. Molecular and biochemical characterization of two brassinosteroid sulfotransferases from Arabidopsis, AtST4a (At2g14920) and AtST1 (At2g03760). Planta. 2007 Apr;225(5):1233-44. Epub 2006 Oct 13. PMID:17039368 doi:http://dx.doi.org/10.1007/s00425-006-0413-y
- ↑ Baek D, Pathange P, Chung JS, Jiang J, Gao L, Oikawa A, Hirai MY, Saito K, Pare PW, Shi H. A stress-inducible sulphotransferase sulphonates salicylic acid and confers pathogen resistance in Arabidopsis. Plant Cell Environ. 2010 Aug 1;33(8):1383-92. doi:, 10.1111/j.1365-3040.2010.02156.x. Epub 2010 Apr 1. PMID:20374532 doi:http://dx.doi.org/10.1111/j.1365-3040.2010.02156.x
