2rj4

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[[Image:2rj4.jpg|left|200px]]
[[Image:2rj4.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2rj4 |SIZE=350|CAPTION= <scene name='initialview01'>2rj4</scene>, resolution 1.470&Aring;
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The line below this paragraph, containing "STRUCTURE_2rj4", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+A+2'>AC1</scene>, <scene name='pdbsite=AC2:Udp+Binding+Site+For+Residue+A+1'>AC2</scene> and <scene name='pdbsite=AC3:Ad7+Binding+Site+For+Residue+A+356'>AC3</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AD7:OCTYL+3-AMINO-3-DEOXY-2-O-(2,6-DIDEOXY-ALPHA-L-LYXO-HEXOPYRANOSYL)-BETA-D-GALACTOPYRANOSIDE'>AD7</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5&#39;-DIPHOSPHATE'>UDP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fucosylgalactoside_3-alpha-galactosyltransferase Fucosylgalactoside 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.37 2.4.1.37] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2rj4| PDB=2rj4 | SCENE= }}
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|RELATEDENTRY=[[2rit|2RIT]], [[2rix|2RIX]], [[2riy|2RIY]], [[2riz|2RIZ]], [[2rj0|2RJ0]], [[2rj1|2RJ1]], [[2rj5|2RJ5]], [[2rj6|2RJ6]], [[2rj7|2RJ7]], [[2rj8|2RJ8]], [[2rj9|2RJ9]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rj4 OCA], [http://www.ebi.ac.uk/pdbsum/2rj4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rj4 RCSB]</span>
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}}
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'''B-specific alpha-1,3-galactosyltransferase \ G176R +UDP+ADA'''
'''B-specific alpha-1,3-galactosyltransferase \ G176R +UDP+ADA'''
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[[Category: Alfaro, J A.]]
[[Category: Alfaro, J A.]]
[[Category: Evans, S V.]]
[[Category: Evans, S V.]]
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[[Category: blood group antigen]]
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[[Category: Blood group antigen]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: glycosyltransferase]]
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[[Category: Glycosyltransferase]]
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[[Category: golgi apparatus]]
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[[Category: Golgi apparatus]]
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[[Category: gtb abo rossman fold bbbb unliganded]]
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[[Category: Gtb abo rossman fold bbbb unliganded]]
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[[Category: manganese]]
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[[Category: Manganese]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: secreted]]
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[[Category: Secreted]]
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[[Category: signal-anchor]]
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[[Category: Signal-anchor]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:00:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:01:02 2008''
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Revision as of 14:00, 4 May 2008

Image:2rj4.jpg

Template:STRUCTURE 2rj4

B-specific alpha-1,3-galactosyltransferase \ G176R +UDP+ADA


Contents

Overview

The final step in the enzymatic synthesis of the ABO(H) blood group A and B antigens is catalyzed by two closely related glycosyltransferases, an a-(1-3)-N-acetylgalactosaminyltransferase (GTA) and an a-(1-3)-galactosyltransferase (GTB). Of their 354 amino acid residues, GTA and GTB differ by only four 'critical' residues. High-resolution structures for GTB and the GTA/GTB chimeric enzymes GTB/G176R and GTB/G176R/G235S bound to a panel of donor and acceptor analog substrates reveal 'open', 'semi-closed' and 'closed' conformations as the enzymes go from the unliganded to the liganded states. In the 'open' form the internal polypeptide loop (amino acid residues 177-195) adjacent to the active site in the unliganded or H-antigen-bound enzymes is composed of two a-helices spanning Arg180-Met186 and Arg188-Asp194 respectively. The 'semi-closed' and closed forms of the enzymes are generated by binding of UDP or of UDP and H-antigen analogs respectively, and show that these helices merge to form a single distorted helical structure with alternating a-310-a character that partially occludes the active site. The 'closed' form is distinguished from the 'semi-closed' form by the ordering of the final nine C-terminal residues through the formation of hydrogen bonds to both UDP and H-antigen analogs. The 'semi-closed' forms for various mutants generally show significantly more disorder than the 'open' forms, while the 'closed' forms display little or no disorder depending strongly on the identity of residue 176. Finally, the use of synthetic analogs reveals how H-antigen acceptor binding can be critical in stabilizing the 'closed' conformation. These structures demonstrate a delicately-balanced substrate recognition mechanism and give insight on critical aspects of donor and acceptor specificity, on the order of substrate binding, and on the requirements for catalysis.

Disease

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

About this Structure

2RJ4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes., Alfaro JA, Zheng RB, Persson M, Letts JA, Polakowski R, Bai Y, Borisova SN, Seto NO, Lowary TL, Palcic MM, Evans SV, J Biol Chem. 2008 Jan 11;. PMID:18192272 Page seeded by OCA on Sun May 4 17:00:35 2008

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OCA

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