1rh1: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1rh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh1, resolution 2.5Å" /> '''crystal structure of ...
 
OCA (talk | contribs)
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1rh1.gif|left|200px]]<br /><applet load="1rh1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rh1, resolution 2.5&Aring;" />
'''crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution'''<br />


==Overview==
==crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution==
Colicin B (55 kDa) is a cytotoxic protein that recognizes the outer, membrane transporter, FepA, as a receptor and, after gaining access to the, cytoplasmic membranes of sensitive Escherichia coli cells, forms a pore, that depletes the electrochemical potential of the membrane and ultimately, results in cell death. To begin to understand the series of dynamic, conformational changes that must occur as colicin B translocates from, outer membrane to cytoplasmic membrane, we report here the crystal, structure of colicin B at 2.5 A resolution. The crystal belongs to the, space group C2221 with unit cell dimensions a = 132.162 A, b = 138.167 A, c = 106.16 A. The overall structure of colicin B is dumbbell shaped., Unlike colicin Ia, the only other TonB-dependent colicin crystallized to, date, colicin B does not have clearly structurally delineated, receptor-binding and translocation domains. Instead, the unique N-terminal, lobe of the dumbbell contains both domains and consists of a large (290, residues), mostly beta-stranded structure with two short alpha-helices., This is followed by a single long ( approximately 74 A) helix that, connects the N-terminal domain to the C-terminal pore-forming domain, which is composed of 10 alpha-helices arranged in a bundle-type structure, similar to the pore-forming domains of other colicins. The TonB box, sequence at the N-terminus folds back to interact with the N-terminal lobe, of the dumbbell and leaves the flanking sequences highly disordered., Comparison of sequences among many colicins has allowed the identification, of a putative receptor-binding domain.
<StructureSection load='1rh1' size='340' side='right'caption='[[1rh1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh1 OCA], [https://pdbe.org/1rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEAB_ECOLX CEAB_ECOLX]


==About this Structure==
==See Also==
1RH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RH1 OCA].
*[[Colicin 3D structures|Colicin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution., Hilsenbeck JL, Park H, Chen G, Youn B, Postle K, Kang C, Mol Microbiol. 2004 Feb;51(3):711-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14731273 14731273]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chen, G.]]
[[Category: Chen G]]
[[Category: Hilsenbeck, J.L.]]
[[Category: Hilsenbeck JL]]
[[Category: Kang, C.]]
[[Category: Kang C]]
[[Category: Park, H.]]
[[Category: Park H]]
[[Category: Postle, K.]]
[[Category: Postle K]]
[[Category: Youn, B.]]
[[Category: Youn B]]
[[Category: colicin b]]
[[Category: crystal structure]]
[[Category: cytotoxic bacterial protein]]
[[Category: fepa]]
[[Category: tonb]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:29 2007''

Latest revision as of 08:22, 14 February 2024

crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution

1rh1, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA