Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid

Jennifer R. Fleming; Alice Dawson; William N. Hunter

doi:10.1016/j.molbiopara.2010.08.002

Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid

Jennifer R. Fleming, Alice Dawson, William N. Hunter

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

6 Citations (Scopus)

Abstract

ADP-ribosylation factor-like (ARL) proteins are small GTPases that undergo conformational changes upon nucleotide binding, and which regulate the affinity of ARLs for binding other proteins, lipids or membranes. There is a paucity of structural data on this family of proteins in the Kinetoplastida, despite studies implicating them in key events related to vesicular transport and regulation of microtubule-dependent processes. The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 angstrom resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Putative L. major and Trypanosoma brucei ARF/ARL family members have been classified based on structural considerations, amino acid sequence conservation combined with functional data on Kinetoplastid and human orthologues. This classification may guide future studies designed to elucidate the function of specific family members. (C) 2010 Elsevier B.V. All rights reserved

Original language	English
Pages (from-to)	141-144
Number of pages	4
Journal	Molecular and Biochemical Parasitology
Volume	174
Issue number	2
DOIs	https://doi.org/10.1016/j.molbiopara.2010.08.002
Publication status	Published - Dec 2010

Keywords

ADP-ribosylation factor-like
GTPase
Leishmania
Protein structure
ARF FAMILY
BINDING PROTEINS
SAR PROTEINS
TRAFFICKING
INFERENCE
VIABILITY
NETWORK
ROLES

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10.1016/j.molbiopara.2010.08.002

Aref#d: 19815. Wellcome Trust Centre for Drug Discovery (Strategic Award)
Fairlamb, A., Ferguson, M. & Frearson, J.
Wellcome Trust
1/01/08 → 31/12/12
Project: Research
Aref#d: 19401. Structure, specificity and mechanism of biosynthetic enzymes in trypanosomatids and inhibitor discovery of essential microbial functions (Programme Grant)
Hunter, B.
Wellcome Trust
1/11/07 → 31/12/13
Project: Research

Cite this

@article{643c585a6c7d4b1a84f2f82e1a3f868d,

title = "Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid",

abstract = "ADP-ribosylation factor-like (ARL) proteins are small GTPases that undergo conformational changes upon nucleotide binding, and which regulate the affinity of ARLs for binding other proteins, lipids or membranes. There is a paucity of structural data on this family of proteins in the Kinetoplastida, despite studies implicating them in key events related to vesicular transport and regulation of microtubule-dependent processes. The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 angstrom resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Putative L. major and Trypanosoma brucei ARF/ARL family members have been classified based on structural considerations, amino acid sequence conservation combined with functional data on Kinetoplastid and human orthologues. This classification may guide future studies designed to elucidate the function of specific family members. (C) 2010 Elsevier B.V. All rights reserved",

keywords = "ADP-ribosylation factor-like, GTPase, Leishmania, Protein structure, ARF FAMILY, BINDING PROTEINS, SAR PROTEINS, TRAFFICKING, INFERENCE, VIABILITY, NETWORK, ROLES",

author = "Fleming, {Jennifer R.} and Alice Dawson and Hunter, {William N.}",

year = "2010",

month = dec,

doi = "10.1016/j.molbiopara.2010.08.002",

language = "English",

volume = "174",

pages = "141--144",

journal = "Molecular and Biochemical Parasitology",

issn = "0166-6851",

publisher = "Elsevier",

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}

TY - JOUR

T1 - Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid

AU - Fleming, Jennifer R.

AU - Dawson, Alice

AU - Hunter, William N.

PY - 2010/12

Y1 - 2010/12

N2 - ADP-ribosylation factor-like (ARL) proteins are small GTPases that undergo conformational changes upon nucleotide binding, and which regulate the affinity of ARLs for binding other proteins, lipids or membranes. There is a paucity of structural data on this family of proteins in the Kinetoplastida, despite studies implicating them in key events related to vesicular transport and regulation of microtubule-dependent processes. The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 angstrom resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Putative L. major and Trypanosoma brucei ARF/ARL family members have been classified based on structural considerations, amino acid sequence conservation combined with functional data on Kinetoplastid and human orthologues. This classification may guide future studies designed to elucidate the function of specific family members. (C) 2010 Elsevier B.V. All rights reserved

AB - ADP-ribosylation factor-like (ARL) proteins are small GTPases that undergo conformational changes upon nucleotide binding, and which regulate the affinity of ARLs for binding other proteins, lipids or membranes. There is a paucity of structural data on this family of proteins in the Kinetoplastida, despite studies implicating them in key events related to vesicular transport and regulation of microtubule-dependent processes. The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 angstrom resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Putative L. major and Trypanosoma brucei ARF/ARL family members have been classified based on structural considerations, amino acid sequence conservation combined with functional data on Kinetoplastid and human orthologues. This classification may guide future studies designed to elucidate the function of specific family members. (C) 2010 Elsevier B.V. All rights reserved

KW - ADP-ribosylation factor-like

KW - GTPase

KW - Leishmania

KW - Protein structure

KW - ARF FAMILY

KW - BINDING PROTEINS

KW - SAR PROTEINS

KW - TRAFFICKING

KW - INFERENCE

KW - VIABILITY

KW - NETWORK

KW - ROLES

U2 - 10.1016/j.molbiopara.2010.08.002

DO - 10.1016/j.molbiopara.2010.08.002

M3 - Article

SN - 0166-6851

VL - 174

SP - 141

EP - 144

JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

IS - 2

ER -

Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid

Abstract

Keywords

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Projects

Aref#d: 19815. Wellcome Trust Centre for Drug Discovery (Strategic Award)

Aref#d: 19401. Structure, specificity and mechanism of biosynthetic enzymes in trypanosomatids and inhibitor discovery of essential microbial functions (Programme Grant)

Cite this