Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution

Laura-Lee Clancy Kelley; Bret D. Dillard; Wolfram Tempel; Lirong Chen; Neil Shaw; Doowon Lee; M. Gary Newton; Frank J. Sugar; Francis E. Jenney; Han Seung Lee; Claudia Shah; Farris L. Poole; Michael W. W. Adams; Jane S. Richardson; David C. Richardson; Zhi-Jie Liu; Bi-Cheng Wang; John Rose

Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution

Laura-Lee Clancy Kelley
, Bret D. Dillard
, Wolfram Tempel
, Lirong Chen
, Neil Shaw
, Doowon Lee
, M. Gary Newton
, Frank J. Sugar
, Francis E. Jenney
, Han Seung Lee
, Claudia Shah
, Farris L. Poole
, Michael W. W. Adams
, Jane S. Richardson
, David C. Richardson
, Zhi-Jie Liu
, Bi-Cheng Wang
, John Rose

Department of Bio-Medical Sciences (PCOM)

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

Abstract

The hypothetical protein PF0899 is a 95-residue peptide from the hyperthermophilic archaeon Pyrococcus furiosus that represents a gene family with six members. P. furiosus ORF PF0899 has been cloned, expressed and crystallized and its structure has been determined by the Southeast Collaboratory for Structural Genomics (http://www.secsg.org). The structure was solved using the SCA2Structure pipeline from multiple data sets and has been refined to 1.85 A against the highest resolution data set collected (a presumed gold derivative), with a crystallographic R factor of 21.0% and R(free) of 24.0%. The refined structure shows some structural similarity to a wedge-shaped domain observed in the structure of the major capsid protein from bacteriophage HK97, suggesting that PF0899 may be a structural protein.

Original language	American English
Journal	Acta Crystallographica Section F, Structural Biology and Crystallization Communications
Volume	63
State	Published - Jul 1 2007

Keywords

Archaeal Proteins
Cloning
Molecular
Crystallization
Crystallography
X-Ray
Open Reading Frames
Protein Structure
Secondary
Pyrococcus furiosus

Disciplines

Genomics
Medicine and Health Sciences
Structural Biology

Cite this

Kelley, L.-L. C., Dillard, B. D., Tempel, W., Chen, L., Shaw, N., Lee, D., Newton, M. G., Sugar, F. J., Jenney, F. E., Lee, H. S., Shah, C., Poole, F. L., Adams, M. W. W., Richardson, J. S., Richardson, D. C., Liu, Z.-J., Wang, B.-C., & Rose, J. (2007). Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution. Acta Crystallographica Section F, Structural Biology and Crystallization Communications, 63.

Kelley, L-LC, Dillard, BD, Tempel, W, Chen, L, Shaw, N, Lee, D, Newton, MG, Sugar, FJ, Jenney, FE, Lee, HS, Shah, C, Poole, FL, Adams, MWW, Richardson, JS, Richardson, DC, Liu, Z-J, Wang, B-C & Rose, J 2007, 'Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution', Acta Crystallographica Section F, Structural Biology and Crystallization Communications, vol. 63.

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title = "Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution",

abstract = " The hypothetical protein PF0899 is a 95-residue peptide from the hyperthermophilic archaeon Pyrococcus furiosus that represents a gene family with six members. P. furiosus ORF PF0899 has been cloned, expressed and crystallized and its structure has been determined by the Southeast Collaboratory for Structural Genomics (http://www.secsg.org). The structure was solved using the SCA2Structure pipeline from multiple data sets and has been refined to 1.85 A against the highest resolution data set collected (a presumed gold derivative), with a crystallographic R factor of 21.0\% and R(free) of 24.0\%. The refined structure shows some structural similarity to a wedge-shaped domain observed in the structure of the major capsid protein from bacteriophage HK97, suggesting that PF0899 may be a structural protein.",

keywords = "Archaeal Proteins, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Open Reading Frames, Protein Structure, Secondary, Pyrococcus furiosus",

author = "Kelley, \{Laura-Lee Clancy\} and Dillard, \{Bret D.\} and Wolfram Tempel and Lirong Chen and Neil Shaw and Doowon Lee and Newton, \{M. Gary\} and Sugar, \{Frank J.\} and Jenney, \{Francis E.\} and Lee, \{Han Seung\} and Claudia Shah and Poole, \{Farris L.\} and Adams, \{Michael W. W.\} and Richardson, \{Jane S.\} and Richardson, \{David C.\} and Zhi-Jie Liu and Bi-Cheng Wang and John Rose",

year = "2007",

month = jul,

day = "1",

language = "American English",

volume = "63",

journal = "Acta Crystallographica Section F, Structural Biology and Crystallization Communications",

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TY - JOUR

T1 - Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution

AU - Kelley, Laura-Lee Clancy

AU - Dillard, Bret D.

AU - Tempel, Wolfram

AU - Chen, Lirong

AU - Shaw, Neil

AU - Lee, Doowon

AU - Newton, M. Gary

AU - Sugar, Frank J.

AU - Jenney, Francis E.

AU - Lee, Han Seung

AU - Shah, Claudia

AU - Poole, Farris L.

AU - Adams, Michael W. W.

AU - Richardson, Jane S.

AU - Richardson, David C.

AU - Liu, Zhi-Jie

AU - Wang, Bi-Cheng

AU - Rose, John

PY - 2007/7/1

Y1 - 2007/7/1

N2 - The hypothetical protein PF0899 is a 95-residue peptide from the hyperthermophilic archaeon Pyrococcus furiosus that represents a gene family with six members. P. furiosus ORF PF0899 has been cloned, expressed and crystallized and its structure has been determined by the Southeast Collaboratory for Structural Genomics (http://www.secsg.org). The structure was solved using the SCA2Structure pipeline from multiple data sets and has been refined to 1.85 A against the highest resolution data set collected (a presumed gold derivative), with a crystallographic R factor of 21.0% and R(free) of 24.0%. The refined structure shows some structural similarity to a wedge-shaped domain observed in the structure of the major capsid protein from bacteriophage HK97, suggesting that PF0899 may be a structural protein.

AB - The hypothetical protein PF0899 is a 95-residue peptide from the hyperthermophilic archaeon Pyrococcus furiosus that represents a gene family with six members. P. furiosus ORF PF0899 has been cloned, expressed and crystallized and its structure has been determined by the Southeast Collaboratory for Structural Genomics (http://www.secsg.org). The structure was solved using the SCA2Structure pipeline from multiple data sets and has been refined to 1.85 A against the highest resolution data set collected (a presumed gold derivative), with a crystallographic R factor of 21.0% and R(free) of 24.0%. The refined structure shows some structural similarity to a wedge-shaped domain observed in the structure of the major capsid protein from bacteriophage HK97, suggesting that PF0899 may be a structural protein.

KW - Archaeal Proteins

KW - Cloning

KW - Molecular

KW - Crystallization

KW - Crystallography

KW - X-Ray

KW - Open Reading Frames

KW - Protein Structure

KW - Secondary

KW - Pyrococcus furiosus

UR - https://digitalcommons.pcom.edu/scholarly_papers/200

M3 - Article

VL - 63

JO - Acta Crystallographica Section F, Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F, Structural Biology and Crystallization Communications

ER -

Structure of the Hypothetical Protein PF0899 from Pyrococcus furiosus at 1.85 A Resolution

Abstract

Keywords

Disciplines

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