1lz0: Difference between revisions

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[[Image:1lz0.gif|left|200px]]<br /><applet load="1lz0" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1lz0.gif|left|200px]]
caption="1lz0, resolution 1.8&Aring;" />
 
'''Glycosyltransferase A'''<br />
{{Structure
|PDB= 1lz0 |SIZE=350|CAPTION= <scene name='initialview01'>1lz0</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40]
|GENE=
}}
 
'''Glycosyltransferase A'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1LZ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZ0 OCA].  
1LZ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZ0 OCA].  


==Reference==
==Reference==
The structural basis for specificity in human ABO(H) blood group biosynthesis., Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV, Nat Struct Biol. 2002 Sep;9(9):685-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12198488 12198488]
The structural basis for specificity in human ABO(H) blood group biosynthesis., Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV, Nat Struct Biol. 2002 Sep;9(9):685-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12198488 12198488]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: transmembrane]]
[[Category: transmembrane]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:45 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:49 2008''

Revision as of 10:36, 20 March 2008

File:1lz0.gif


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1lz0, resolution 1.8Å
Ligands: HG
Activity: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, with EC number 2.4.1.40
Coordinates: save as pdb, mmCIF, xml



Glycosyltransferase A


Overview

The human ABO(H) blood group antigens are produced by specific glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA) uses a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase (GTB) uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. GTA and GTB differ only in the identity of four critical amino acid residues. Crystal structures at 1.8-1.32 A resolution of the GTA and GTB enzymes both free and in complex with disaccharide H-antigen acceptor and UDP reveal the basis for donor and acceptor specificity and show that only two of the critical amino acid residues are positioned to contact donor or acceptor substrates. Given the need for stringent stereo- and regioselectivity in this biosynthesis, these structures further demonstrate that the ability of the two enzymes to distinguish between the A and B donors is largely determined by a single amino acid residue.

Disease

Known disease associated with this structure: Blood group, ABO system OMIM:[110300]

About this Structure

1LZ0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structural basis for specificity in human ABO(H) blood group biosynthesis., Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV, Nat Struct Biol. 2002 Sep;9(9):685-90. PMID:12198488

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