4hu3

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'''Unreleased structure'''
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{{STRUCTURE_4hu3| PDB=4hu3 | SCENE= }}
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===Crystal structure of EAL domain of the E. coli DosP - monomeric form===
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{{ABSTRACT_PUBMED_23695249}}
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The entry 4hu3 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/DOSP_ECOLI DOSP_ECOLI]] Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.<ref>PMID:20553324</ref>
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Authors: Tarnawski, M., Barends, T.R.M., Hartmann, E., Schlichting, I.
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==About this Structure==
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[[4hu3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HU3 OCA].
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Description:
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==Reference==
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<ref group="xtra">PMID:023695249</ref><references group="xtra"/><references/>
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[[Category: Cyclic-guanylate-specific phosphodiesterase]]
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[[Category: Escherichia coli k-12]]
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[[Category: Barends, T R.M.]]
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[[Category: Hartmann, E.]]
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[[Category: Schlichting, I.]]
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[[Category: Tarnawski, M.]]
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[[Category: Cyclic di-gmp phosphodiesterase]]
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[[Category: Direct oxygen sensor]]
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[[Category: Eal domain]]
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[[Category: Ecdo]]
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[[Category: Hydrolase]]
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[[Category: Signaling protein]]
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[[Category: Tim-barrel]]

Revision as of 16:20, 19 June 2013

Template:STRUCTURE 4hu3

Contents

Crystal structure of EAL domain of the E. coli DosP - monomeric form

Template:ABSTRACT PUBMED 23695249

Function

[DOSP_ECOLI] Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.[1]

About this Structure

4hu3 is a 1 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

Reference

  • Tarnawski M, Barends TR, Hartmann E, Schlichting I. Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1045-53. doi:, 10.1107/S0907444913004423. Epub 2013 May 14. PMID:23695249 doi:10.1107/S0907444913004423
  1. ↑ Tagliabue L, Maciag A, Antoniani D, Landini P. The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli. FEMS Immunol Med Microbiol. 2010 Aug;59(3):477-84. doi:, 10.1111/j.1574-695X.2010.00702.x. Epub 2010 May 20. PMID:20553324 doi:10.1111/j.1574-695X.2010.00702.x

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