4br4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 18: Line 18:
</div>
</div>
<div class="pdbe-citations 4br4" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4br4" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 01:16, 16 November 2017

Legionella pneumophila NTPDase1 crystal form I, open, apoLegionella pneumophila NTPDase1 crystal form I, open, apo

Structural highlights

4br4 is a 1 chain structure with sequence from Atcc 33152. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Apyrase, with EC number 3.6.1.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

In vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic site for hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17 degrees .

Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases.,Zebisch M, Krauss M, Schafer P, Lauble P, Strater N Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Zebisch M, Krauss M, Schafer P, Lauble P, Strater N. Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases. Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739 doi:10.1016/j.str.2013.05.016

4br4, resolution 1.45Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA