Sandbox UC 22

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== Your Heading Here (maybe something like 'Structure') ==
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== 1CRX structure ==
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<StructureSection load='1xcd' size='350' side='right' caption='Structure of a group fragment(Group_000066)' scene=''>
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{{STRUCTURE_1crx| PDB=1crx | SCENE= }}
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Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core of decorin, the best characterized member of the SLRP family. Each monomer adopts the curved solenoid fold characteristic of LRR domains, with a parallel beta-sheet on the inside interwoven with loops containing short segments of beta-strands, 3(10) helices, and polyproline II helices on the outside. Two main features are unique to this structure. First, decorin dimerizes through the concave surfaces of the LRR domains, which have been implicated previously in protein-ligand interactions. The amount of surface buried in this dimer rivals the buried surfaces of some of the highest-affinity macromolecular complexes reported to date. Second, the C-terminal region adopts an unusual capping motif that involves a laterally extended LRR and a disulfide bond. This motif seems to be unique to SLRPs and has not been observed in any other LRR protein structure to date. Possible implications of these features for decorin ligand binding and SLRP function are discussed.
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</StructureSection>
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<h1>Protein cluster</h1>
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<h1>Structure of CRE Recombinase/DNA Complex Reaction intermediate I</h1>
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{{ABSTRACT_PUBMED_9288963}}

Current revision

1CRX structure

PDB ID 1crx

Drag the structure with the mouse to rotate
1crx, resolution 2.40Å ()
Ligands:
Gene: CRE (Enterobacteria phage P1)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of CRE Recombinase/DNA Complex Reaction intermediate I


Publication Abstract from PubMed

During site-specific DNA recombination, which brings about genetic rearrangement in processes such as viral integration and excision and chromosomal segregation, recombinase enzymes recognize specific DNA sequences and catalyse the reciprocal exchange of DNA strands between these sites. The bacteriophage recombinase Cre catalyses site-specific recombination between two 34-base-pair loxP sites. The crystal structure at 2.4 A resolution of Cre bound to a loxP substrate reveals an intermediate in the recombination reaction, in which a Cre molecule has cleaved the substrate to form a covalent 3'-phosphotyrosine linkage with the DNA. Four recombinases and two loxP sites form a synapsed structure in which the DNA resembles models of four-way Holliday-Junction intermediates. The Cre-loxP complex challenges models of site-specific recombination that require large changes in quaternary structure. Subtle allosteric changes at the carboxy termini of the Cre subunits may instead coordinate the cleavage and strand-exchange reactions.

Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse., Guo F, Gopaul DN, van Duyne GD, Nature. 1997 Sep 4;389(6646):40-6. PMID:9288963

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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