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dc.contributor.authorPark, Mi Seul
Bitto, Eduard
Kim, Kyung Rok
Bingman, Craig A.
Miller, Mitchell D.
Kim, Hyun-Jung
Han, Byung Woo
Phillips, George N. Jr.
dc.date.accessioned 2015-01-06T19:20:33Z
dc.date.available 2015-01-06T19:20:33Z
dc.date.issued 2014
dc.identifier.citation Park, Mi Seul, Bitto, Eduard, Kim, Kyung Rok, et al.. "Crystal Structure of Human Protein N-Terminal Glutamine Amidohydrolase, an Initial Component of the N-End Rule Pathway." PLoS ONE, 9, no. 10 (2014) Public Library of Science: e111142. http://dx.doi.org/10.1371/journal.pone.0111142.
dc.identifier.urihttps://hdl.handle.net/1911/78894
dc.description.abstract The N-end rule states that half-life of protein is determined by their N-terminal amino acid residue. N-terminal glutamine amidohydrolase (Ntaq) converts N-terminal glutamine to glutamate by eliminating the amine group and plays an essential role in the N-end rule pathway for protein degradation. Here, we report the crystal structure of human Ntaq1 bound with the N-terminus of a symmetry-related Ntaq1 molecule at 1.5 Å resolution. The structure reveals a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. The N-terminus of a symmetry-related Ntaq1 molecule bound in the substrate binding cleft and the active site suggest possible substrate binding mode of hNtaq1. Based on our crystal structure of hNtaq1 and docking study with all the tripeptides with N-terminal glutamine, we propose how the peptide backbone recognition patch of hNtaq1 forms nonspecific interactions with N-terminal peptides of substrate proteins. Upon binding of a substrate with N-terminal glutamine, active site catalytic triad mediates the deamination of the N-terminal residue to glutamate by a mechanism analogous to that of cysteine proteases.
dc.language.iso eng
dc.publisher Public Library of Science
dc.rights This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.title Crystal Structure of Human Protein N-Terminal Glutamine Amidohydrolase, an Initial Component of the N-End Rule Pathway
dc.type Journal article
dc.citation.journalTitle PLoS ONE
dc.citation.volumeNumber 9
dc.citation.issueNumber 10
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0111142
dc.identifier.pmcid PMC4214742
dc.identifier.pmid 25356641
dc.type.publication publisher version
dc.citation.firstpage e111142


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This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Except where otherwise noted, this item's license is described as This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.