4nkg

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'''Unreleased structure'''
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{{STRUCTURE_4nkg| PDB=4nkg | SCENE= }}
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===Crystal structure of SspH1 LRR domain in complex PKN1 HR1b domain===
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{{ABSTRACT_PUBMED_24248594}}
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The entry 4nkg is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/SSPH1_SALT1 SSPH1_SALT1]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host PKN1. Down-modulates production of host proinflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression, probably via interaction with PKN1.<ref>PMID:10564523</ref> <ref>PMID:12819095</ref> <ref>PMID:16611232</ref> <ref>PMID:18005683</ref> [[http://www.uniprot.org/uniprot/PKN1_HUMAN PKN1_HUMAN]] PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.<ref>PMID:8557118</ref> <ref>PMID:8621664</ref> <ref>PMID:9175763</ref> <ref>PMID:11104762</ref> <ref>PMID:12514133</ref> <ref>PMID:17332740</ref> <ref>PMID:18066052</ref> <ref>PMID:20188095</ref> <ref>PMID:21754995</ref>
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Authors: Keszei, A.F.A., Xiaojing, T., Mccormick, C., Zeqiraj, E., Rohde, J.R., Tyers, M., Sicheri, F.
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==About this Structure==
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[[4nkg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKG OCA].
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Description: Crystal structure of SspH1 LRR domain in complex PKN1 HR1b domain
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==Reference==
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<ref group="xtra">PMID:024248594</ref><references group="xtra"/><references/>
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[[Category: Protein kinase C]]
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[[Category: Keszei, A F.A.]]
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[[Category: Mccormick, C.]]
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[[Category: Rohde, J R.]]
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[[Category: Sicheri, F.]]
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[[Category: Tyers, M.]]
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[[Category: Xiaojing, T.]]
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[[Category: Zeqiraj, E.]]
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[[Category: Coiled-coil]]
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[[Category: E3 ligase substrate interaction]]
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[[Category: Leucine-rich repeat]]
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[[Category: Ligase-transferase complex]]

Revision as of 13:35, 11 December 2013

Template:STRUCTURE 4nkg

Contents

Crystal structure of SspH1 LRR domain in complex PKN1 HR1b domain

Template:ABSTRACT PUBMED 24248594

Function

[SSPH1_SALT1] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host PKN1. Down-modulates production of host proinflammatory cytokines by inhibiting NF-kappa-B-dependent gene expression, probably via interaction with PKN1.[1] [2] [3] [4] [PKN1_HUMAN] PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.[5] [6] [7] [8] [9] [10] [11] [12] [13]

About this Structure

4nkg is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Keszei AF, Tang X, McCormick C, Zeqiraj E, Rohde JR, Tyers M, Sicheri F. Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 2013 Nov 18. PMID:24248594 doi:http://dx.doi.org/10.1128/MCB.01360-13
  1. ↑ Miao EA, Scherer CA, Tsolis RM, Kingsley RA, Adams LG, Baumler AJ, Miller SI. Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems. Mol Microbiol. 1999 Nov;34(4):850-64. PMID:10564523
  2. ↑ Haraga A, Miller SI. A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-kappa B-dependent gene expression. Infect Immun. 2003 Jul;71(7):4052-8. PMID:12819095
  3. ↑ Haraga A, Miller SI. A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1. Cell Microbiol. 2006 May;8(5):837-46. PMID:16611232 doi:http://dx.doi.org/10.1111/j.1462-5822.2005.00670.x
  4. ↑ Rohde JR, Breitkreutz A, Chenal A, Sansonetti PJ, Parsot C. Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Cell Host Microbe. 2007 Mar 15;1(1):77-83. PMID:18005683 doi:10.1016/j.chom.2007.02.002
  5. ↑ Palmer RH, Schonwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ. PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. FEBS Lett. 1996 Jan 15;378(3):281-5. PMID:8557118
  6. ↑ Mukai H, Toshimori M, Shibata H, Kitagawa M, Shimakawa M, Miyahara M, Sunakawa H, Ono Y. PKN associates and phosphorylates the head-rod domain of neurofilament protein. J Biol Chem. 1996 Apr 19;271(16):9816-22. PMID:8621664
  7. ↑ Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M. Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN. Biochem Biophys Res Commun. 1997 May 29;234(3):621-5. PMID:9175763 doi:http://dx.doi.org/10.1006/bbrc.1997.6669
  8. ↑ Taniguchi T, Kawamata T, Mukai H, Hasegawa H, Isagawa T, Yasuda M, Hashimoto T, Terashima A, Nakai M, Mori H, Ono Y, Tanaka C. Phosphorylation of tau is regulated by PKN. J Biol Chem. 2001 Mar 30;276(13):10025-31. Epub 2000 Dec 4. PMID:11104762 doi:http://dx.doi.org/10.1074/jbc.M007427200
  9. ↑ Metzger E, Muller JM, Ferrari S, Buettner R, Schule R. A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer. EMBO J. 2003 Jan 15;22(2):270-80. PMID:12514133 doi:http://dx.doi.org/10.1093/emboj/cdg023
  10. ↑ Schmidt A, Durgan J, Magalhaes A, Hall A. Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis. EMBO J. 2007 Mar 21;26(6):1624-36. Epub 2007 Mar 1. PMID:17332740 doi:http://dx.doi.org/10.1038/sj.emboj.7601637
  11. ↑ Metzger E, Yin N, Wissmann M, Kunowska N, Fischer K, Friedrichs N, Patnaik D, Higgins JM, Potier N, Scheidtmann KH, Buettner R, Schule R. Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Nat Cell Biol. 2008 Jan;10(1):53-60. Epub 2007 Dec 9. PMID:18066052 doi:http://dx.doi.org/10.1038/ncb1668
  12. ↑ Harrison BC, Huynh K, Lundgaard GL, Helmke SM, Perryman MB, McKinsey TA. Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases. FEBS Lett. 2010 Mar 19;584(6):1103-10. doi: 10.1016/j.febslet.2010.02.057. Epub, 2010 Feb 24. PMID:20188095 doi:http://dx.doi.org/10.1016/j.febslet.2010.02.057
  13. ↑ Lachmann S, Jevons A, De Rycker M, Casamassima A, Radtke S, Collazos A, Parker PJ. Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration. PLoS One. 2011;6(7):e21732. doi: 10.1371/journal.pone.0021732. Epub 2011 Jul 6. PMID:21754995 doi:http://dx.doi.org/10.1371/journal.pone.0021732

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