1sc5

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[[Image:1sc5.gif|left|200px]]
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{{Seed}}
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[[Image:1sc5.png|left|200px]]
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{{STRUCTURE_1sc5| PDB=1sc5 | SCENE= }}
{{STRUCTURE_1sc5| PDB=1sc5 | SCENE= }}
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'''Sigma-28(FliA)/FlgM complex'''
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===Sigma-28(FliA)/FlgM complex===
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==Overview==
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The key regulators of bacterial transcription initiation are the sigma factors, which direct promoter recognition and melting but only after binding to the core RNA polymerase to form the holoenzyme. X-ray crystal structures of the flagellar sigma, sigma(28), in complex with its anti-sigma, FlgM, explain the inhibition mechanism of FlgM, including its ability to attack and destabilize the sigma(28)-holoenzyme. The sigma domains (sigma(2), sigma(3), and sigma(4)) pack together in a compact unit with extensive interdomain interfaces that bury the promoter binding determinants, including the -35 element recognition helix of sigma(4), which fits in an acidic groove on the surface of sigma(3). The structure illustrates the large rearrangements that sigma(28) must undergo to form the holoenzyme and provides insights into the regulation of sigma(28) promoter binding activity that may extend, at least in principle, to other sigmas.
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(as it appears on PubMed at http://www.pubmed.gov), where 15068809 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15068809}}
==About this Structure==
==About this Structure==
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[[Category: Rna polymerase sigma factor]]
[[Category: Rna polymerase sigma factor]]
[[Category: Transcription]]
[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:32:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:37:47 2008''

Revision as of 01:37, 28 July 2008

Template:STRUCTURE 1sc5

Sigma-28(FliA)/FlgM complex

Template:ABSTRACT PUBMED 15068809

About this Structure

1SC5 is a Protein complex structure of sequences from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation., Sorenson MK, Ray SS, Darst SA, Mol Cell. 2004 Apr 9;14(1):127-38. PMID:15068809

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