Waters Timothy R, Eryilmaz Jitka, Geddes Stella, Barrett Tracey E
The School of Crystallography and the Institute for Structural Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, United Kingdom.
FEBS Lett. 2006 Nov 27;580(27):6423-7. doi: 10.1016/j.febslet.2006.10.051. Epub 2006 Nov 3.
UvrB is the damage recognition element of the highly conserved UvrABC pathway that functions in the removal of bulky DNA adducts. Pivotal to this is the formation of a damage detection complex that relies on the ability of UvrB to locate and sequester diverse lesions. Whilst structures of UvrB bound to DNA have recently been reported, none address the issue of lesion recognition. Here, we describe the crystal structure of UvrB bound to a pentanucleotide containing a single fluorescein-adducted thymine that reveals a unique mechanism for damage detection entirely dependent on the exclusion of lesions larger than an undamaged nucleotide.
UvrB是高度保守的UvrABC途径中的损伤识别元件，该途径在去除大分子DNA加合物中发挥作用。关键在于形成一种损伤检测复合物，这依赖于UvrB定位和隔离各种损伤的能力。虽然最近报道了UvrB与DNA结合的结构，但没有一个涉及损伤识别问题。在这里，我们描述了UvrB与含有单个荧光素加合胸腺嘧啶的五核苷酸结合的晶体结构，该结构揭示了一种完全依赖于排除比未损伤核苷酸大的损伤来进行损伤检测的独特机制。
