1ush: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1ush.jpg|left|200px]]<br /><applet load="1ush" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ush.jpg|left|200px]]
caption="1ush, resolution 1.73&Aring;" />
 
'''5'-NUCLEOTIDASE FROM E. COLI'''<br />
{{Structure
|PDB= 1ush |SIZE=350|CAPTION= <scene name='initialview01'>1ush</scene>, resolution 1.73&Aring;
|SITE= <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5]
|GENE= USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''5'-NUCLEOTIDASE FROM E. COLI'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1USH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CO3:'>CO3</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] Known structural/functional Site: <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USH OCA].  
1USH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USH OCA].  


==Reference==
==Reference==
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site., Knofel T, Strater N, Nat Struct Biol. 1999 May;6(5):448-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10331872 10331872]
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site., Knofel T, Strater N, Nat Struct Biol. 1999 May;6(5):448-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331872 10331872]
[[Category: 5'-nucleotidase]]
[[Category: 5'-nucleotidase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 24: Line 33:
[[Category: udp-sugar hydrolase]]
[[Category: udp-sugar hydrolase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:48 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:36:08 2008''

Revision as of 12:36, 20 March 2008

File:1ush.jpg


Drag the structure with the mouse to rotate
1ush, resolution 1.73Å
Sites: ZNB
Ligands: ZN, CO3 and SO4
Gene: USHA (Escherichia coli)
Activity: 5'-nucleotidase, with EC number 3.1.3.5
Coordinates: save as pdb, mmCIF, xml



5'-NUCLEOTIDASE FROM E. COLI


Overview

The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.

About this Structure

1USH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site., Knofel T, Strater N, Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872

Page seeded by OCA on Thu Mar 20 14:36:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA