1wsz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wsz.gif|left|200px]]<br /><applet load="1wsz" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1wsz.gif|left|200px]]
-
caption="1wsz, resolution 1.59&Aring;" />
+
 
-
'''Mutant human ABO(H) blood group transferase A'''<br />
+
{{Structure
 +
|PDB= 1wsz |SIZE=350|CAPTION= <scene name='initialview01'>1wsz</scene>, resolution 1.59&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=
 +
}}
 +
 
 +
'''Mutant human ABO(H) blood group transferase A'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1WSZ 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=1WSZ OCA].
+
1WSZ 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=1WSZ OCA].
==Reference==
==Reference==
-
Structural basis for the inactivity of human blood group O2 glycosyltransferase., Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM, J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15475562 15475562]
+
Structural basis for the inactivity of human blood group O2 glycosyltransferase., Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM, J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15475562 15475562]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 28: Line 37:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:46 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:01:08 2008''

Revision as of 13:01, 20 March 2008


PDB ID 1wsz

Drag the structure with the mouse to rotate
, resolution 1.59Å
Ligands:
Activity: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, with EC number 2.4.1.40
Coordinates: save as pdb, mmCIF, xml



Mutant human ABO(H) blood group transferase A


Contents

Overview

The human ABO(H) blood group antigens are carbohydrate structures generated by glycosyltransferase enzymes. Glycosyltransferase A (GTA) uses UDP-GalNAc as a donor to transfer a monosaccharide residue to Fuc alpha1-2Gal beta-R (H)-terminating acceptors. Similarly, glycosyltransferase B (GTB) catalyzes the transfer of a monosaccharide residue from UDP-Gal to the same acceptors. These are highly homologous enzymes differing in only four of 354 amino acids, Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268. Blood group O usually stems from the expression of truncated inactive forms of GTA or GTB. Recently, an O(2) enzyme was discovered that was a full-length form of GTA with three mutations, P74S, R176G, and G268R. We showed previously that the R176G mutation increased catalytic activity with minor effects on substrate binding. Enzyme kinetics and high resolution structural studies of mutant enzymes based on the O(2) blood group transferase reveal that whereas the P74S mutation in the stem region of the protein does not appear to play a role in enzyme inactivation, the G268R mutation completely blocks the donor GalNAc-binding site leaving the acceptor binding site unaffected.

Disease

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

About this Structure

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

Reference

Structural basis for the inactivity of human blood group O2 glycosyltransferase., Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM, J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. PMID:15475562

Page seeded by OCA on Thu Mar 20 15:01:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools