1veq: Difference between revisions
New page: left|200px<br /><applet load="1veq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1veq, resolution 3.98Å" /> '''Mycobacterium smegma... |
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[[Image:1veq.gif|left|200px]]<br /><applet load="1veq" size=" | [[Image:1veq.gif|left|200px]]<br /><applet load="1veq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1veq, resolution 3.98Å" /> | caption="1veq, resolution 3.98Å" /> | ||
'''Mycobacterium smegmatis Dps Hexagonal form'''<br /> | '''Mycobacterium smegmatis Dps Hexagonal form'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the DNA binding protein from starved cells from | The structure of the DNA binding protein from starved cells from Mycobacterium smegmatis has been determined in three crystal forms and has been compared with those of similar proteins from other sources. The dodecameric molecule can be described as a distorted icosahedron. The interfaces among subunits are such that the dodecameric molecule appears to have been made up of stable trimers. The situation is similar in the proteins from Escherichia coli and Agrobacterium tumefaciens, which are closer to the M.smegmatis protein in sequence and structure than those from other sources, which appear to form a dimer first. Trimerisation is aided in the three proteins by the additional N-terminal stretches that they possess. The M.smegmatis protein has an additional C-terminal stretch compared to other related proteins. The stretch, known to be involved in DNA binding, is situated on the surface of the molecule. A comparison of the available structures permits a delineation of the rigid and flexible regions in the molecule. The subunit interfaces around the molecular dyads, where the ferroxidation centres are located, are relatively rigid. Regions in the vicinity of the acidic holes centred around molecular 3-fold axes, are relatively flexible. So are the DNA binding regions. The crystal structures of the protein from M.smegmatis confirm that DNA molecules can occupy spaces within the crystal without disturbing the arrangement of the protein molecules. However, contrary to earlier suggestions, the spaces do not need to be between layers of protein molecules. The cubic form provides an arrangement in which grooves, which could hold DNA molecules, criss-cross the crystal. | ||
==About this Structure== | ==About this Structure== | ||
1VEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1VEQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VEQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:30 2008'' | ||
Revision as of 16:34, 21 February 2008
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Mycobacterium smegmatis Dps Hexagonal form
OverviewOverview
The structure of the DNA binding protein from starved cells from Mycobacterium smegmatis has been determined in three crystal forms and has been compared with those of similar proteins from other sources. The dodecameric molecule can be described as a distorted icosahedron. The interfaces among subunits are such that the dodecameric molecule appears to have been made up of stable trimers. The situation is similar in the proteins from Escherichia coli and Agrobacterium tumefaciens, which are closer to the M.smegmatis protein in sequence and structure than those from other sources, which appear to form a dimer first. Trimerisation is aided in the three proteins by the additional N-terminal stretches that they possess. The M.smegmatis protein has an additional C-terminal stretch compared to other related proteins. The stretch, known to be involved in DNA binding, is situated on the surface of the molecule. A comparison of the available structures permits a delineation of the rigid and flexible regions in the molecule. The subunit interfaces around the molecular dyads, where the ferroxidation centres are located, are relatively rigid. Regions in the vicinity of the acidic holes centred around molecular 3-fold axes, are relatively flexible. So are the DNA binding regions. The crystal structures of the protein from M.smegmatis confirm that DNA molecules can occupy spaces within the crystal without disturbing the arrangement of the protein molecules. However, contrary to earlier suggestions, the spaces do not need to be between layers of protein molecules. The cubic form provides an arrangement in which grooves, which could hold DNA molecules, criss-cross the crystal.
About this StructureAbout this Structure
1VEQ is a Single protein structure of sequence from Mycobacterium smegmatis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules., Roy S, Gupta S, Das S, Sekar K, Chatterji D, Vijayan M, J Mol Biol. 2004 Jun 18;339(5):1103-13. PMID:15178251
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