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You may include any references to papers as in: the use of the phage structure in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Introduction

The VRR-Nuc (Virus type replication repair nuclease) is a domain found in different enzymes of both eukaryotes and prokaryotes, including humans, bacteria and pages. The VRR-Nuc domain belongs to the phosphodiesterase superfamily PD(D/E)xK, which is a widespread family that contains nucleases with most diverse functions, including, but not restricted to, DNA repair and modification, restriction endonucleases, RNA modification, holiday junction resolvases and, most recently, bacterial antagonist effectors. ^[3][4]

Structural Highlights

The VRR-Nuc containing proteins, since belonging to the PD(D/E)xK superfamily, present structure similar to the core structure of the superfamily. The conserved core includes αβββαβ, in which the conserved residues responsible for the nuclease activity D (Aspartic Acid), D/E (Glutamic Acid), K (Lysine) are usually found in the second and third β-sheets.^[5] The VRR-Nuc containing proteins might present a single domain, only the VRR-Nuc domain (Examples), or present multiple domain proteins (examples FAN1).

Enzymatic Activities

5’ flap single strand degradation (FAN1 ad paFAN1) Holliday Junction resolvase, cutting double-strand four-way DNA (phage and bacteria)

Biological Function

One of the first characterized VRR-Nuc containing proteins is the human FANC1 protein (Fanconi anemia-associated nuclease). This enzyme is composed by many domains (exemplos dos domínios), mainly associated to substrate identification and binding, and FANC1 is responsible for inter-strand crosslinking repair in the DNA, in which the VRR-Nuc participates through exo and endonuclease activity in 5’ flap single strand DNA. Descrever melhor mecanismo de reparo- é a unica com estrutura e função biológica claramente descrito

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