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A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution (173 visite)

Vergara A, Grassi M, Sica F, Pizzo E, D’Alessio G, Mazzarella L, Merlino A

Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 960-967.

Tipo di articolo: Journal Article, , Impact factor: 7.232, Impact factor a 5 anni: 9.416, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84878290879&partnerID=40&md5=d28c3350ceacccc399d02f1acafc68fa

Parole chiave: Atomic Resolution, Calcium Binding, Crystallins, Domain Interactions, Folding, Greek-Key Motif, Trp Corner, Tyr Corner, Animal, Article, Binding Site, Chemical Structure, Chemistry, Genetics, Geodia, Metabolism, Molecular Evolution, Protein Folding, Protein Motif, X Ray Crystallography, Amino Acid Motifs, X-Ray, Models, Geodia Cydonium, Metazoa, Vertebrata,

Affiliazioni: *** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini (CNR), Via Mezzocannone 16, Napoli, Italy
Dipartimento di Biologia, Università Degli Studi di Napoli Federico II, Via Cintia, Napoli, Italy


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The βγ-crystallin superfamily includes highly diverse proteins belonging to all of the kingdoms of life. Based on structural topology, these proteins are considered to be evolutionarily related to the long-lived βγ-crystallins that constitute the vertebrate eye lens. This study reports the crystallographic structure at 0.99 14;Å resolution of the two-domain βγ-crystallin (geodin) from the sponge Geodia cydonium. This is the most ancient member of the βγ-crystallin superfamily in metazoans. The X-ray structure shows that the geodin domains adopt the typical βγ-crystallin fold with a paired Greek-key motif, thus confirming the hypothesis that the crystallin-type scaffold used in the evolution of bacteria and moulds was recruited very early in metazoans. As a significant new structural feature, the sponge protein possesses a unique interdomain interface made up by pairing between the second motif of the first domain and the first motif of the second domain. The atomic resolution also allowed a detailed analysis of the calcium-binding site of the protein. © 2013 International Union of Crystallography.
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Ruggiero A, Chambery A, Di Maro A, Parente A, Berisio R
* Atomic Resolution (1. 1 Angstrom) Structure Of The Ribosome-Inactivating Protein Pd-L4 From Phytolacca Dioica L. Leaves (111 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2008 Apr; 71(1): 8-15.
Impact Factor: 3.419
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Esposito L, Vitagliano L, Mazzarella L
* Recent advances in atomic resolution protein crystallography (108 visite)
Protein And Peptide Letters (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 95-105.
Impact Factor: 0.622
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Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic resolution structures of ribonuclease A at six pH values (198 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002; 58(3): 441-450.
Impact Factor: 1.76
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Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L
* Atomic Resolution Structures Of Rnase A At Six Ph Values (87 visite)
Acta Crystallogr D Biol Crystallogr, 2002; N/D: 441-450.
Impact Factor: 7.232
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Berisio R, Viguera A, Serrano L, Wilmanns M
* Atomic resolution structure of a mutant of the spectrin SH3 domain (86 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Feb; 57(2): 337-340.
Impact Factor: 2.124
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Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
Experimental evidence at atomic resolution for intramolecular N- H···π (phenyl) interactions in a family of amino acid derivatives (118 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
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6 Records (6 escludendo Abstract e Conferenze).
Impact factor totale: 17.582 (17.582 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 36.354 (36.354 escludendo Abstract e Conferenze).







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