1adu

<table><tr><td colspan='2'>[[1adu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ADU FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1adu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adu OCA], [http://pdbe.org/1adu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1adu RCSB], [http://www.ebi.ac.uk/pdbsum/1adu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1adu ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DNB2_ADE05 DNB2_ADE05]] Binds cooperatively single-stranded DNA in a sequence-independent manner. Involved in DNA-replication, regulation of mRNA formation, and host-range specificity. Zinc is required for DNA binding.

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== Publication Abstract from PubMed ==

A second crystal form of the C-terminal domain of the adenovirus single-stranded DNA binding protein crystallizes in space group P2(1)2(1)2(1) with a=61.0 angstrom, b=91.2 angstrom and c=149.4 angstrom. The crystals contain two molecules per asymmetric unit and diffract to a maximum resolution of 3.0 angstrom. The crystal is composed of infinite chains of molecules along the crystallographic 2(1) axis parallel to c. The principal intermolecular interaction is a hooking of the C-terminal 17 residues of one molecule onto the next molecule in the protein chain. Adjacent molecules in the chain are rotated approximately 90 degrees with respect to their neighbours. The difference in relative orientation of adjacent molecules between the two crystal forms of the protein implies a degree of flexibility in the protein chain that would facilitate DNA binding.

Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein.,Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA J Mol Biol. 1996 Mar 22;257(1):1-8. PMID:8632448<ref>PMID:8632448</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1adu" style="background-color:#fffaf0;"></div>

*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]]

[[Category: Kanellopoulos, P N]]

[[Category: Tsernoglou, D]]

[[Category: Tucker, P A]]

[[Category: Vliet, P C.Van Der]]

[[Category: Ssdna binding protein]]