4edv

<StructureSection load='4edv' size='340' side='right' caption='[[4edv]], [[Resolution|resolution]] 2.01&Aring;' scene=''>

<table><tr><td colspan='2'>[[4edv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EDV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0O2:GUANOSINE+5-(TETRAHYDROGEN+TRIPHOSPHATE)+3-(TRIHYDROGEN+DIPHOSPHATE)'>0O2</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e2k|4e2k]], [[4ee1|4ee1]], [[4edz|4edz]], [[4edy|4edy]], [[4edt|4edt]], [[4edr|4edr]]</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=4edv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4edv RCSB], [http://www.ebi.ac.uk/pdbsum/4edv PDBsum]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Primases are DNA-dependent RNA polymerases found in all cellular organisms. In bacteria, primer synthesis is carried out by DnaG, an essential enzyme that serves as a key component of DNA replication initiation, progression, and restart. How DnaG associates with nucleotide substrates and how certain naturally prevalent nucleotide analogs impair DnaG function are unknown. We have examined one of the earliest stages in primer synthesis and its control by solving crystal structures of the S. aureus DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp. These structures, together with both biochemical analyses and comparative studies of enzymes that use the same catalytic fold as DnaG, pinpoint the predominant nucleotide-binding site of DnaG and explain how the induction of the stringent response in bacteria interferes with primer synthesis.

 

Binding Mechanism of MetalNTP Substrates and Stringent-Response Alarmones to Bacterial DnaG-Type Primases.,Rymer RU, Solorio FA, Tehranchi AK, Chu C, Corn JE, Keck JL, Wang JD, Berger JM Structure. 2012 Jul 10. PMID:22795082<ref>PMID:22795082</ref>

 

*[[RNA polymerase|RNA polymerase]]

[[Category: Berger, J M]]

[[Category: Chu, C]]

[[Category: Corn, J E]]

[[Category: Rymer, R U]]

[[Category: Solorio, F A]]

[[Category: Wang, J D]]

[[Category: Bacterial]]

[[Category: Catalytic domain]]

[[Category: Transferase-transferase inhibitor complex]]