1mt0: Difference between revisions
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|PDB= 1mt0 |SIZE=350|CAPTION= <scene name='initialview01'>1mt0</scene>, resolution 2.6Å | |PDB= 1mt0 |SIZE=350|CAPTION= <scene name='initialview01'>1mt0</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HLYB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= HLYB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt0 OCA], [http://www.ebi.ac.uk/pdbsum/1mt0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mt0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Schmitt, L.]] | [[Category: Schmitt, L.]] | ||
[[Category: Stubbs, M T.]] | [[Category: Stubbs, M T.]] | ||
[[Category: abc-transporter]] | [[Category: abc-transporter]] | ||
[[Category: atp-binding domain]] | [[Category: atp-binding domain]] | ||
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[[Category: haemolysin b]] | [[Category: haemolysin b]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:55 2008'' | ||
Revision as of 22:20, 30 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Gene: | HLYB (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATP-binding domain of haemolysin B from Escherichia coli
OverviewOverview
The ABC-transporter haemolysin B is a central component of the secretion machinery that translocates the toxin, haemolysin A, in a Sec-independent fashion across both membranes of E. coli. Here, we report the X-ray crystal structure of the nucleotide-binding domain (NBD) of HlyB. The molecule shares the common overall architecture of ABC-transporter NBDs. However, the last three residues of the Walker A motif adopt a 3(10) helical conformation, stabilized by a bound anion. In consequence, this results in an unusual interaction between the Walker A lysine residue and the Walker B glutamate residue. As these residues are normally required to be available for ATP binding, for catalysis and for dimer formation of ABC domains, we suggest that this conformation may represent a latent monomeric form of the NBD. Surprisingly, comparison of available NBD structures revealed a structurally diverse region (SDR) of about 30 residues within the helical arm II domain, unique to each of the eight NBDs analyzed. As this region interacts with the transmembrane part of ABC-transporters, the SDR helps to explain the selectivity and/or targeting of different NBDs to their cognate transmembrane domains.
About this StructureAbout this Structure
1MT0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains., Schmitt L, Benabdelhak H, Blight MA, Holland IB, Stubbs MT, J Mol Biol. 2003 Jul 4;330(2):333-42. PMID:12823972
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