4HJP

SHP-1 catalytic domain WPD loop open

Summary for 4HJP

• Entry DOI: 10.2210/pdb4hjp/pdb
• Related: 4HJQ
• Descriptor: Tyrosine-protein phosphatase non-receptor type 6 (2 entities in total)
• Functional Keywords: phosphatase domain, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P29350
• Total number of polymer chains: 1
• Total formula weight: 32934.18

Authors

Alicea-Velazquez, N.L.,Boggon, T.J. (deposition date: 2012-10-13, release date: 2013-04-03, Last modification date: 2023-09-20)

Primary citation

Alicea-Velazquez, N.L.,Boggon, T.J.
SHP Family Protein Tyrosine Phosphatases Adopt Canonical Active-Site Conformations in the Apo and Phosphate-Bound States.
Protein Pept.Lett., 20:1039-1048, 2013

PubMed Abstract: Protein tyrosine phosphatase (PTP) catalytic domains undergo a series of conformational changes in order to mediate dephosphorylation of their tyrosine phosphorylated substrates. An important conformational change occurs in the Tryptophan-Proline-Aspartic acid (WPD) loop, which contains the conserved catalytic aspartate. Upon substrate binding, the WPD loop transitions from the 'open' to the 'closed' state, thus allowing optimal positioning of the catalytic aspartate for substrate dephosphorylation. The dynamics of WPD loop conformational changes have previously been studied for PTP1B, HePTP, and the bacterial phosphatase YopH, but have not yet been comprehensively studied for the nonreceptor tyrosine phosphatase SHP-1 (PTPN6). To structurally describe the changes in WPD loop conformation in SHP-1, we have determined the 1.4 Å crystal structure of the catalytic domain of SHP-1 in the Apo state and the 1.8 Å crystal structure of the SHP-1 catalytic domain in complex with a phosphate ion. We provide structural analysis for the WPD loop closed state of SHP phosphatases and the conformational changes that occur upon WPD loop closure.

PubMed: 23514039

Experimental method

X-RAY DIFFRACTION (1.3994 Å)