4bes

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'''Unreleased structure'''
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{{STRUCTURE_4bes| PDB=4bes | SCENE= }}
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===Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein in complex with cytidine monophosphate and phosphocholine===
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{{ABSTRACT_PUBMED_23572077}}
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The entry 4bes is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/ANKX_LEGPH ANKX_LEGPH]] Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine transferase by mediating the addition of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C) and RAB35, leading to displacement of GDP dissociation inhibitors (GDI). Phosphocholination of target proteins also impairs accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.<ref>PMID:18566289</ref> <ref>PMID:22158903</ref> <ref>PMID:21822290</ref> <ref>PMID:22307087</ref> <ref>PMID:22411835</ref>
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Authors: Campanacci, V., Mukherjee, S., Roy, C.R., Cherfils, J.
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==About this Structure==
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[[4bes]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._philadelphia_1 Legionella pneumophila subsp. pneumophila str. philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BES OCA].
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Description: Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein in complex with cytidine monophosphate and phosphocholine
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]]
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[[Category: Campanacci, V.]]
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[[Category: Cherfils, J.]]
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[[Category: Mukherjee, S.]]
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[[Category: Roy, C R.]]
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[[Category: Phosphocholination]]
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[[Category: Transferase]]
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[[Category: Type iv secretion system effector]]

Revision as of 11:22, 24 April 2013

Template:STRUCTURE 4bes

Contents

Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein in complex with cytidine monophosphate and phosphocholine

Template:ABSTRACT PUBMED 23572077

Function

[ANKX_LEGPH] Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine transferase by mediating the addition of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C) and RAB35, leading to displacement of GDP dissociation inhibitors (GDI). Phosphocholination of target proteins also impairs accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.[1] [2] [3] [4] [5]

About this Structure

4bes is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. philadelphia 1. Full crystallographic information is available from OCA.

Reference

  1. ↑ Pan X, Luhrmann A, Satoh A, Laskowski-Arce MA, Roy CR. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science. 2008 Jun 20;320(5883):1651-4. doi: 10.1126/science.1158160. PMID:18566289 doi:10.1126/science.1158160
  2. ↑ Tan Y, Arnold RJ, Luo ZQ. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):21212-7. doi:, 10.1073/pnas.1114023109. Epub 2011 Dec 7. PMID:22158903 doi:10.1073/pnas.1114023109
  3. ↑ Mukherjee S, Liu X, Arasaki K, McDonough J, Galan JE, Roy CR. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature. 2011 Aug 7;477(7362):103-6. doi: 10.1038/nature10335. PMID:21822290 doi:10.1038/nature10335
  4. ↑ Goody PR, Heller K, Oesterlin LK, Muller MP, Itzen A, Goody RS. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J. 2012 Feb 3;31(7):1774-84. doi: 10.1038/emboj.2012.16. PMID:22307087 doi:10.1038/emboj.2012.16
  5. ↑ Oesterlin LK, Goody RS, Itzen A. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5621-6. doi:, 10.1073/pnas.1121161109. Epub 2012 Mar 12. PMID:22411835 doi:10.1073/pnas.1121161109

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