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	===Domains===		===Domains===
-	PHPT1 contains 2 acetylation site and a N-acetylalanine site	+	PHPT1 contains acetylation site and a N-acetylalanine site.
	There is also an Janus/Ocnus family region, characteristic.		There is also an Janus/Ocnus family region, characteristic.
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-	= Disease =	+	= Diseases and medical applications =
-	= Relevance =
	= Structural highlights =		= Structural highlights =

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Revision as of 15:48, 30 January 2016

spinqualitylabelsall models Human Phosphohistidine phosphatase 1 (Homotrimer) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Human Phosphohistidine phosphatase 1

This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159.

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(Human) Phosphohistidine phosphatase 1 belongs to the Janus family, and has 2 isoforms produced by alternative splicing, and 6 transcripts. It is encoded by the PHPT1 gene, located on the 9th chromosome.

Contents 1 Structure 1.1 Generality 1.2 Domains 2 Function 2.1 Ligands and binding 3 Diseases and medical applications 4 Structural highlights 4.1 References

Structure

spinqualitylabelsall models Solution structure of a Human Phosphohistidine Phosphatase 1 monomer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Generality

Phosphohistidine phosphatase 1 is a 14kDa homotrimeric protein, which monomers contain all 125 amino acids. Furthermore, one monomer contains 4 α helices, 6 β strands and 2 turns.

Domains

PHPT1 contains acetylation site and a N-acetylalanine site. There is also an Janus/Ocnus family region, characteristic.

It has one substrate binding site, and one proton acceptor active site.

Function

It is an hydrolase. This characteristic structure allows it to have many activities : phosphoprotein and phosphohistidine phosphatase, calcium channel inhibition, ion channel binding. It is located in the cytosol and in extracellular exosome.

Ligands and binding

There are 6 SO4 lingands, called SO4 201 to 206. 2 lingand fix to each monomer (2ai6), inducing a conformational change of all the monomers (2hw4). Then, the fix lingands bind to each other, forming a trimer (2NMM). O4 S is a 96 Da molecule, with two negative charges. The four oxygens allow good fixation on the monomers, with hydrogen bounds.

Diseases and medical applications

Structural highlights

</StructureSection>

References