Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0

Zoë Fisher; Andrey Y. Kovalevsky; Marat Mustyakimov; David N. Silverman; Robert McKenna; Paul Langan

doi:10.1021/bi201487b

Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0

Zoë Fisher, Andrey Y. Kovalevsky, Marat Mustyakimov, David N. Silverman, Robert McKenna, Paul Langan

Single Crystal Diffraction

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.

Original language	English
Pages (from-to)	9421-9423
Number of pages	3
Journal	Biochemistry
Volume	50
Issue number	44
DOIs	https://doi.org/10.1021/bi201487b
State	Published - Nov 8 2011

Access to Document

10.1021/bi201487b

Cite this

@article{2109c5c63a2b45c89b84a9d57eae6040,

title = "Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network {"}switch{"} is observed between pH 7.8 and 10.0",

abstract = "The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 {\AA} resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.",

author = "Zo{\"e} Fisher and Kovalevsky, {Andrey Y.} and Marat Mustyakimov and Silverman, {David N.} and Robert McKenna and Paul Langan",

year = "2011",

month = nov,

day = "8",

doi = "10.1021/bi201487b",

language = "English",

volume = "50",

pages = "9421--9423",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "44",

}

TY - JOUR

T1 - Neutron structure of human carbonic anhydrase II

T2 - A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0

AU - Fisher, Zoë

AU - Kovalevsky, Andrey Y.

AU - Mustyakimov, Marat

AU - Silverman, David N.

AU - McKenna, Robert

AU - Langan, Paul

PY - 2011/11/8

Y1 - 2011/11/8

N2 - The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.

AB - The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.

UR - http://www.scopus.com/inward/record.url?scp=80155203797&partnerID=8YFLogxK

U2 - 10.1021/bi201487b

DO - 10.1021/bi201487b

M3 - Article

C2 - 21988105

AN - SCOPUS:80155203797

SN - 0006-2960

VL - 50

SP - 9421

EP - 9423

JO - Biochemistry

JF - Biochemistry

IS - 44

ER -

Neutron structure of human carbonic anhydrase II: A hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0

Abstract

Access to Document

Other files and links

Fingerprint

Cite this