2jmp
From Proteopedia
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| - | [[Image:2jmp.jpg|left|200px]]<br /><applet load="2jmp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2jmp" /> | ||
| - | '''Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium'''<br /> | ||
| - | == | + | ==Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium== |
| + | <StructureSection load='2jmp' size='340' side='right'caption='[[2jmp]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2jmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_genitalium Mycoplasma genitalium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMP FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmp OCA], [https://pdbe.org/2jmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmp RCSB], [https://www.ebi.ac.uk/pdbsum/2jmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DNAA_MYCGE DNAA_MYCGE] Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
DnaA is an essential component in the initiation of bacterial chromosomal replication. DnaA binds to a series of 9 base pair repeats leading to oligomerization, recruitment of the DnaBC helicase, and the assembly of the replication fork machinery. The structure of the N-terminal domain (residues 1-100) of DnaA from Mycoplasma genitalium was determined by NMR spectroscopy. The backbone r.m.s.d. for the first 86 residues was 0.6 +/- 0.2 A based on 742 NOE, 50 hydrogen bond, 46 backbone angle, and 88 residual dipolar coupling restraints. Ultracentrifugation studies revealed that the domain is monomeric in solution. Features on the protein surface include a hydrophobic cleft flanked by several negative residues on one side, and positive residues on the other. A negatively charged ridge is present on the opposite face of the protein. These surfaces may be important sites of interaction with other proteins involved in the replication process. Together, the structure and NMR assignments should facilitate the design of new experiments to probe the protein-protein interactions essential for the initiation of DNA replication. | DnaA is an essential component in the initiation of bacterial chromosomal replication. DnaA binds to a series of 9 base pair repeats leading to oligomerization, recruitment of the DnaBC helicase, and the assembly of the replication fork machinery. The structure of the N-terminal domain (residues 1-100) of DnaA from Mycoplasma genitalium was determined by NMR spectroscopy. The backbone r.m.s.d. for the first 86 residues was 0.6 +/- 0.2 A based on 742 NOE, 50 hydrogen bond, 46 backbone angle, and 88 residual dipolar coupling restraints. Ultracentrifugation studies revealed that the domain is monomeric in solution. Features on the protein surface include a hydrophobic cleft flanked by several negative residues on one side, and positive residues on the other. A negatively charged ridge is present on the opposite face of the protein. These surfaces may be important sites of interaction with other proteins involved in the replication process. Together, the structure and NMR assignments should facilitate the design of new experiments to probe the protein-protein interactions essential for the initiation of DNA replication. | ||
| - | + | NMR structure of the N-terminal domain of the replication initiator protein DnaA.,Lowery TJ, Pelton JG, Chandonia JM, Kim R, Yokota H, Wemmer DE J Struct Funct Genomics. 2007 Mar;8(1):11-7. Epub 2007 Aug 7. PMID:17680349<ref>PMID:17680349</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2jmp" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[DnaA|DnaA]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycoplasma genitalium]] | ||
| + | [[Category: Lowery TJ]] | ||
| + | [[Category: Pelton JG]] | ||
| + | [[Category: Wemmer DE]] | ||
Current revision
Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium
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