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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1wai.png|left|200px]]
 
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==DNA POLYMERASE FROM BACTERIOPHAGE RB69, ALPHA-CARBONS ONLY, WITH DNA MODELED IN THE POLYMERASE ACTIVE SITE, THEORETICAL MODEL==
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The line below this paragraph, containing "STRUCTURE_1wai", creates the "Structure Box" on the page.
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<StructureSection load='1wai' size='340' side='right'caption='[[1wai]]' 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'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1wai FirstGlance], [https://www.ebi.ac.uk/pdbsum/1wai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wai ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1wai| PDB=1wai | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 2.8 A resolution crystal structure of the bacteriophage RB69 gp43, a member of the eukaryotic pol alpha family of replicative DNA polymerases, shares some similarities with other polymerases but shows many differences. Although its palm domain has the same topology as other polymerases, except rat DNA polymerase beta, one of the three carboxylates required for nucleotidyl transfer is located on a different beta strand. The structures of the fingers and thumb domains are unrelated to all other known polymerase structures. The editing 3'-5' exonuclease domain of gp43 is homologous to that of E. coli DNA polymerase I but lies on the opposite side of the polymerase active site. An extended structure-based alignment of eukaryotic DNA polymerase sequences provides structural insights that should be applicable to most eukaryotic DNA polymerases.
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===DNA POLYMERASE FROM BACTERIOPHAGE RB69, ALPHA-CARBONS ONLY, WITH DNA MODELED IN THE POLYMERASE ACTIVE SITE, THEORETICAL MODEL===
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Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69.,Wang J, Sattar AK, Wang CC, Karam JD, Konigsberg WH, Steitz TA Cell. 1997 Jun 27;89(7):1087-99. PMID:9215631<ref>PMID:9215631</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_9215631}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1wai" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 9215631 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9215631}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAI OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:9215631</ref><references group="xtra"/>
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[[Category: Karam, J D]]
[[Category: Karam, J D]]
[[Category: Konigsberg, W H]]
[[Category: Konigsberg, W H]]
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[[Category: Wang, C C]]
[[Category: Wang, C C]]
[[Category: Wang, J]]
[[Category: Wang, J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:59:06 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

DNA POLYMERASE FROM BACTERIOPHAGE RB69, ALPHA-CARBONS ONLY, WITH DNA MODELED IN THE POLYMERASE ACTIVE SITE, THEORETICAL MODEL

PDB ID 1wai

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