X-ray Crystal Structure of Divalent Metal-Activated β-xylosidase, RS223BX

Douglas B. Jordan; Jay D. Braker; Kurt Wagschal; Charles C. Lee; Victor J. Chan; Ievgeniia Dubrovska; Spencer M Anderson; Zdzislaw Wawrzak

doi:10.1007/s12010-015-1767-z

X-ray Crystal Structure of Divalent Metal-Activated β-xylosidase, RS223BX

Douglas B. Jordan^*, Jay D. Braker, Kurt Wagschal, Charles C. Lee, Victor J. Chan, Ievgeniia Dubrovska, Spencer M Anderson, Zdzislaw Wawrzak

^*Corresponding author for this work

Pharmacology

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

16 Scopus citations

Abstract

We report the X-ray crystal structure of a glycoside hydrolase family 43 β-xylosidase, RS223BX, which is strongly activated by the addition of divalent metal cations. The 2.69 Å structure reveals that the Ca²⁺ cation is located at the back of the active-site pocket. The Ca²⁺ is held in the active site by the carboxylate of D85, an “extra” acid residue in comparison to other GH43 active sites. The Ca²⁺ is in close contact with a histidine imidazole, which in turn is in contact with the catalytic base (D15) thus providing a mechanism for stabilizing the carboxylate anion of the base and achieve metal activation. The active-site pocket is mirrored by an “inactive-site” pocket of unknown function that resides on the opposite side of the monomer.

Original language	English (US)
Pages (from-to)	637-648
Number of pages	12
Journal	Applied Biochemistry and Biotechnology
Volume	177
Issue number	3
DOIs	https://doi.org/10.1007/s12010-015-1767-z
State	Published - Oct 30 2015

Keywords

Activation
Divalent metal cations
GH43 β-xylosidase
Inverting mechanism

ASJC Scopus subject areas

Applied Microbiology and Biotechnology
Bioengineering
Molecular Biology
Biochemistry
Biotechnology

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@article{7e86720183854b30bef36e340aa64812,

title = "X-ray Crystal Structure of Divalent Metal-Activated β-xylosidase, RS223BX",

abstract = "We report the X-ray crystal structure of a glycoside hydrolase family 43 β-xylosidase, RS223BX, which is strongly activated by the addition of divalent metal cations. The 2.69 {\AA} structure reveals that the Ca2+ cation is located at the back of the active-site pocket. The Ca2+ is held in the active site by the carboxylate of D85, an “extra” acid residue in comparison to other GH43 active sites. The Ca2+ is in close contact with a histidine imidazole, which in turn is in contact with the catalytic base (D15) thus providing a mechanism for stabilizing the carboxylate anion of the base and achieve metal activation. The active-site pocket is mirrored by an “inactive-site” pocket of unknown function that resides on the opposite side of the monomer.",

keywords = "Activation, Divalent metal cations, GH43 β-xylosidase, Inverting mechanism",

author = "Jordan, {Douglas B.} and Braker, {Jay D.} and Kurt Wagschal and Lee, {Charles C.} and Chan, {Victor J.} and Ievgeniia Dubrovska and Anderson, {Spencer M} and Zdzislaw Wawrzak",

note = "Publisher Copyright: {\textcopyright} 2015, Springer Science+Business Media New York (outside the USA).",

year = "2015",

month = oct,

day = "30",

doi = "10.1007/s12010-015-1767-z",

language = "English (US)",

volume = "177",

pages = "637--648",

journal = "Applied Biochemistry and Biotechnology",

issn = "0273-2289",

publisher = "Springer",

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TY - JOUR

T1 - X-ray Crystal Structure of Divalent Metal-Activated β-xylosidase, RS223BX

AU - Jordan, Douglas B.

AU - Braker, Jay D.

AU - Wagschal, Kurt

AU - Lee, Charles C.

AU - Chan, Victor J.

AU - Dubrovska, Ievgeniia

AU - Anderson, Spencer M

AU - Wawrzak, Zdzislaw

PY - 2015/10/30

Y1 - 2015/10/30

N2 - We report the X-ray crystal structure of a glycoside hydrolase family 43 β-xylosidase, RS223BX, which is strongly activated by the addition of divalent metal cations. The 2.69 Å structure reveals that the Ca2+ cation is located at the back of the active-site pocket. The Ca2+ is held in the active site by the carboxylate of D85, an “extra” acid residue in comparison to other GH43 active sites. The Ca2+ is in close contact with a histidine imidazole, which in turn is in contact with the catalytic base (D15) thus providing a mechanism for stabilizing the carboxylate anion of the base and achieve metal activation. The active-site pocket is mirrored by an “inactive-site” pocket of unknown function that resides on the opposite side of the monomer.

AB - We report the X-ray crystal structure of a glycoside hydrolase family 43 β-xylosidase, RS223BX, which is strongly activated by the addition of divalent metal cations. The 2.69 Å structure reveals that the Ca2+ cation is located at the back of the active-site pocket. The Ca2+ is held in the active site by the carboxylate of D85, an “extra” acid residue in comparison to other GH43 active sites. The Ca2+ is in close contact with a histidine imidazole, which in turn is in contact with the catalytic base (D15) thus providing a mechanism for stabilizing the carboxylate anion of the base and achieve metal activation. The active-site pocket is mirrored by an “inactive-site” pocket of unknown function that resides on the opposite side of the monomer.

KW - Activation

KW - Divalent metal cations

KW - GH43 β-xylosidase

KW - Inverting mechanism

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U2 - 10.1007/s12010-015-1767-z

DO - 10.1007/s12010-015-1767-z

M3 - Article

C2 - 26201482

AN - SCOPUS:84942549881

SN - 0273-2289

VL - 177

SP - 637

EP - 648

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

IS - 3

ER -

X-ray Crystal Structure of Divalent Metal-Activated β-xylosidase, RS223BX

Abstract

Keywords

ASJC Scopus subject areas

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