1rda

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[[Image:1rda.jpg|left|200px]]
 
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==CRYSTAL STRUCTURES OF RIBONUCLEASE HI ACTIVE SITE MUTANTS FROM ESCHERICHIA COLI==
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The line below this paragraph, containing "STRUCTURE_1rda", creates the "Structure Box" on the page.
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<StructureSection load='1rda' size='340' side='right'caption='[[1rda]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rda]] 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=1RDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RDA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rda OCA], [https://pdbe.org/1rda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rda RCSB], [https://www.ebi.ac.uk/pdbsum/1rda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rda ProSAT]</span></td></tr>
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{{STRUCTURE_1rda| PDB=1rda | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNH_ECOLI RNH_ECOLI] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. RNase H participates in DNA replication; it helps to specify the origin of genomic replication by suppressing initiation at origins other than the oriC locus; along with the 5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki fragments of lagging strand synthesis; and it defines the origin of replication for ColE1-type plasmids by specific cleavage of an RNA preprimer.[HAMAP-Rule:MF_00042]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/1rda_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rda ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURES OF RIBONUCLEASE HI ACTIVE SITE MUTANTS FROM ESCHERICHIA COLI'''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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In order to investigate the relationships between the three-dimensional structure and the enzymic activity of E. coli RNase HI, three mutant proteins, which were completely inactivated by the replacements of three functional residues, Asp10 by Asn (D10N), Glu48 by Gln (E48Q), and Asp70 by Asn (D70N), were crystallized. Their three-dimensional structures were determined by x-ray crystallography. Although the entire backbone structures of these mutants were not affected by the replacements, very localized conformational changes were observed around the Mg(2+)-binding site. The substitution of an amide group for a negatively charged carboxyl group in common induces the formation of new hydrogen bond networks, presumably due to the cancellation of repulsive forces between carboxyl side chains with negative charges. These conformational changes can account for the loss of the enzymic activity in the mutants, and suggest a possible role for Mg2+ in the hydrolysis. Since the 3 replaced acidic residues are completely conserved in sequences of reverse transcriptases from retroviruses, including human immunodeficiency virus, the concepts of the catalytic mechanism deduced from this structural analysis can also be applied to RNase H activity in reverse transcriptases.
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==About this Structure==
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1RDA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RDA OCA].
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==Reference==
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Crystal structures of ribonuclease HI active site mutants from Escherichia coli., Katayanagi K, Ishikawa M, Okumura M, Ariyoshi M, Kanaya S, Kawano Y, Suzuki M, Tanaka I, Morikawa K, J Biol Chem. 1993 Oct 15;268(29):22092-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8408067 8408067]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Ribonuclease H]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Katayanagi K]]
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[[Category: Katayanagi, K.]]
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[[Category: Morikawa K]]
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[[Category: Morikawa, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:21:31 2008''
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Current revision

CRYSTAL STRUCTURES OF RIBONUCLEASE HI ACTIVE SITE MUTANTS FROM ESCHERICHIA COLI

PDB ID 1rda

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