1isg: Difference between revisions

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[[Image:1isg.gif|left|200px]]
[[Image:1isg.gif|left|200px]]


{{Structure
<!--
|PDB= 1isg |SIZE=350|CAPTION= <scene name='initialview01'>1isg</scene>, resolution 2.60&Aring;
The line below this paragraph, containing "STRUCTURE_1isg", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SAP:ADENOSINE-5&#39;-DIPHOSPHATE+MONOTHIOPHOSPHATE'>SAP</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1isg| PDB=1isg  | SCENE= }}  
|RELATEDENTRY=[[1isf|1ISF]], [[1ish|1ISH]], [[1isi|1ISI]], [[1isj|1ISJ]], [[1ism|1ISM]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isg OCA], [http://www.ebi.ac.uk/pdbsum/1isg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1isg RCSB]</span>
}}


'''Crystal Structure Analysis of BST-1/CD157 with ATPgammaS'''
'''Crystal Structure Analysis of BST-1/CD157 with ATPgammaS'''
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Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities., Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K, J Mol Biol. 2002 Feb 22;316(3):711-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11866528 11866528]
Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities., Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K, J Mol Biol. 2002 Feb 22;316(3):711-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11866528 11866528]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: NAD(+) nucleosidase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ariyoshi, M.]]
[[Category: Ariyoshi, M.]]
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[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: Yamamoto-Katayama, S.]]
[[Category: Yamamoto-Katayama, S.]]
[[Category: adp ribosylcyclase]]
[[Category: Adp ribosylcyclase]]
[[Category: atpgamma]]
[[Category: Atpgamma]]
[[Category: cn]]
[[Category: Cn]]
[[Category: nad glycohydrolase]]
[[Category: Nad glycohydrolase]]
 
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Revision as of 20:21, 2 May 2008

File:1isg.gif

Template:STRUCTURE 1isg

Crystal Structure Analysis of BST-1/CD157 with ATPgammaS


OverviewOverview

cADPR is the novel second messenger that elicits calcium release from intracellular calcium stores and works independently of IP(3). In mammals, the ADP-ribosyl cyclase function is found in two membrane proteins, CD38 and BST-1/CD157. These enzymes, exposed extracellularly, bear cADPR hydrolase and NAD glycohydrolase activities. In spite of its functional importance, the structural basis of these enzymatic reactions remains elusive. We determined the crystal structures of the extracellular region of human BST-1 at atomic resolution in the free form and in complexes with five substrate analogues: nicotinamide, NMN, ATPgammaS, ethenoNADP, and ethenoNAD. The three-dimensional structural views of the reaction centre with these ligands revealed the mode of substrate binding and the catalytic mechanism of the multifunctional enzymatic reactions. In each catalytic cleft of the dimeric enzyme, substrates are recognized predominantly through van der Waals interactions with two tryptophan residues, and thereby the N-glycosidic bond of NAD is correctly exposed near a catalytic glutamate residue. Its carboxyl side-chain stabilizes the catalytic intermediate of the S(N)-1 type reaction. This conformation of the catalytic cleft also implies the mechanism of cyclization between the adenine base and the ribose. The three key residues are invariant among the sequences of BST-1, CD38, and Aplysia cyclase, and hence this substrate recognition mode and catalytic scheme appear to be common in the cyclase family.

About this StructureAbout this Structure

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

ReferenceReference

Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities., Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K, J Mol Biol. 2002 Feb 22;316(3):711-23. PMID:11866528 Page seeded by OCA on Fri May 2 20:21:34 2008

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