1ls6: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1ls6.gif|left|200px]]
{{Seed}}
[[Image:1ls6.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ls6|  PDB=1ls6  |  SCENE=  }}  
{{STRUCTURE_1ls6|  PDB=1ls6  |  SCENE=  }}  


'''Human SULT1A1 complexed with PAP and p-Nitrophenol'''
===Human SULT1A1 complexed with PAP and p-Nitrophenol===




==Overview==
<!--
Sulfonation catalyzed by sulfotransferase enzymes plays an important role in chemical defense mechanisms against various xenobiotics but also bioactivates carcinogens. A major human sulfotransferase, SULT1A1, metabolizes and/or bioactivates many endogenous compounds and is implicated in a range of cancers because of its ability to modify diverse promutagen and procarcinogen xenobiotics. The crystal structure of human SULT1A1 reported here is the first sulfotransferase structure complexed with a xenobiotic substrate. An unexpected finding is that the enzyme accommodates not one but two molecules of the xenobiotic model substrate p-nitrophenol in the active site. This result is supported by kinetic data for SULT1A1 that show substrate inhibition for this small xenobiotic. The extended active site of SULT1A1 is consistent with binding of diiodothyronine but cannot easily accommodate beta-estradiol, although both are known substrates. This observation, together with evidence for a disorder-order transition in SULT1A1, suggests that the active site is flexible and can adapt its architecture to accept diverse hydrophobic substrates with varying sizes, shapes and flexibility. Thus the crystal structure of SULT1A1 provides the molecular basis for substrate inhibition and reveals the first clues as to how the enzyme sulfonates a wide variety of lipophilic compounds.
The line below this paragraph, {{ABSTRACT_PUBMED_12471039}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12471039 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12471039}}


==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Sult 1a1]]
[[Category: Sult 1a1]]
[[Category: Two substrate binding site]]
[[Category: Two substrate binding site]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:14:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:59:36 2008''

Revision as of 18:59, 2 July 2008

File:1ls6.png

Template:STRUCTURE 1ls6

Human SULT1A1 complexed with PAP and p-Nitrophenol

Template:ABSTRACT PUBMED 12471039

About this Structure

1LS6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition., Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, Liyou NE, McManus ME, Martin JL, J Biol Chem. 2003 Feb 28;278(9):7655-62. Epub 2002 Dec 5. PMID:12471039

Page seeded by OCA on Wed Jul 2 21:59:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ls6&oldid=627212"