4zbh: Difference between revisions

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'''Unreleased structure'''
==THE CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF SULFOLOBUS ACIDOCALDARIUS FLAF==
<StructureSection load='4zbh' size='340' side='right' caption='[[4zbh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zbh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZBH FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zbh RCSB], [http://www.ebi.ac.uk/pdbsum/4zbh PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Archaea employ the archaellum, a type IV pilus-like nanomachine, for swimming motility. In the crenarchaeon Sulfolobus acidocaldarius, the archaellum consists of seven proteins: FlaB/X/G/F/H/I/J. FlaF is conserved and essential for archaellum assembly but no FlaF structures exist. Here, we truncated the FlaF N terminus and solved 1.5-A and 1.65-A resolution crystal structures of this monotopic membrane protein. Structures revealed an N-terminal alpha-helix and an eight-strand beta-sandwich, immunoglobulin-like fold with striking similarity to S-layer proteins. Crystal structures, X-ray scattering, and mutational analyses suggest dimer assembly is needed for in vivo function. The sole cell envelope component of S. acidocaldarius is a paracrystalline S-layer, and FlaF specifically bound to S-layer protein, suggesting that its interaction domain is located in the pseudoperiplasm with its N-terminal helix in the membrane. From these data, FlaF may act as the previously unknown archaellum stator protein that anchors the rotating archaellum to the archaeal cell envelope.


The entry 4zbh is ON HOLD
FlaF Is a beta-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein.,Banerjee A, Tsai CL, Chaudhury P, Tripp P, Arvai AS, Ishida JP, Tainer JA, Albers SV Structure. 2015 Apr 3. pii: S0969-2126(15)00079-9. doi:, 10.1016/j.str.2015.03.001. PMID:25865246<ref>PMID:25865246</ref>


Authors: Tsai, C.-L., Arvai, A.S., Ishida, J.P., Tainer, J.A.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: THE CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF SULFOLOBUS ACIDOCALDARIUS FLAF
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Tainer, J.A]]
__TOC__
[[Category: Tsai, C.-L]]
</StructureSection>
[[Category: Arvai, A.S]]
[[Category: Arvai, A S]]
[[Category: Ishida, J.P]]
[[Category: Ishida, J P]]
[[Category: Tainer, J A]]
[[Category: Tsai, C L]]
[[Category: Immune system]]
[[Category: Immunoglobulin-like beta-sandwich]]
[[Category: Stator protein]]

Revision as of 14:39, 30 April 2015

THE CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF SULFOLOBUS ACIDOCALDARIUS FLAFTHE CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF SULFOLOBUS ACIDOCALDARIUS FLAF

Structural highlights

4zbh is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Archaea employ the archaellum, a type IV pilus-like nanomachine, for swimming motility. In the crenarchaeon Sulfolobus acidocaldarius, the archaellum consists of seven proteins: FlaB/X/G/F/H/I/J. FlaF is conserved and essential for archaellum assembly but no FlaF structures exist. Here, we truncated the FlaF N terminus and solved 1.5-A and 1.65-A resolution crystal structures of this monotopic membrane protein. Structures revealed an N-terminal alpha-helix and an eight-strand beta-sandwich, immunoglobulin-like fold with striking similarity to S-layer proteins. Crystal structures, X-ray scattering, and mutational analyses suggest dimer assembly is needed for in vivo function. The sole cell envelope component of S. acidocaldarius is a paracrystalline S-layer, and FlaF specifically bound to S-layer protein, suggesting that its interaction domain is located in the pseudoperiplasm with its N-terminal helix in the membrane. From these data, FlaF may act as the previously unknown archaellum stator protein that anchors the rotating archaellum to the archaeal cell envelope.

FlaF Is a beta-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein.,Banerjee A, Tsai CL, Chaudhury P, Tripp P, Arvai AS, Ishida JP, Tainer JA, Albers SV Structure. 2015 Apr 3. pii: S0969-2126(15)00079-9. doi:, 10.1016/j.str.2015.03.001. PMID:25865246[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Banerjee A, Tsai CL, Chaudhury P, Tripp P, Arvai AS, Ishida JP, Tainer JA, Albers SV. FlaF Is a beta-Sandwich Protein that Anchors the Archaellum in the Archaeal Cell Envelope by Binding the S-Layer Protein. Structure. 2015 Apr 3. pii: S0969-2126(15)00079-9. doi:, 10.1016/j.str.2015.03.001. PMID:25865246 doi:http://dx.doi.org/10.1016/j.str.2015.03.001

4zbh, resolution 1.50Å

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