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Role of hydration in collagen triple helix stabilization
No full textCollagen is the most abundant protein in higher vertebrates. Despite collagen repetitive sequence, several aspects of its structure and stability are controversial. Here we performed molecular dynamics simulations to analyze triple helix hydration in regions characterized by different imino/aminoacid contents. Data emerged from MD simulations show that (a) MD simulations can reliably reproduce the hydration sites identified experimentally, (b) water molecules bound to regions with a different amino/iminoacid content exhibit diversified residence times, and (c) in the aminoacid-rich region the binding of water molecules is strongly influenced by the local sequence of the peptide. MD results also suggest that, in aminoacid-rich regions, the stabilizing effects of Arg and Hyp residues on collagen triple helix also depend on water-mediated interactions. On this basis, we propose that the mechanism of triple helix stabilization is sequence-dependent. © 2008 Elsevier Inc. All rights reserved
Role of hydration in collagen recognition by bacterial adhesins
No full textProtein-protein recognition regulates the vast majority of physiological or pathological processes. We investigated the role of hydration in collagen recognition by bacterial adhesin CNA by means of first principle molecular-dynamics samplings. Our characterization of the hydration properties of the isolated partners highlights dewetting-prone areas on the surface of CNA that closely match the key regions involved in hydrophobic intermolecular interactions upon complex formation, suggesting that the hydration state of the ligand-free CNA predisposes the protein to the collagen recognition. Moreover, hydration maps of the CNA-collagen complex reveal the presence of a number of structured water molecules that mediate intermolecular interactions at the interface between the two proteins. These hydration sites feature long residence times, significant binding free energies, and a geometrical distribution that closely resembles the hydration pattern of the isolated collagen triple helix. These findings are striking evidence that CNA recognizes the collagen triple helix as a hydrated molecule. For this structural motif, the exposure of several unsatisfied backbone carbonyl groups results in a strong interplay with the solvent, which is shown to also play a role in collagen recognition. © 2011 by the Biophysical Society
CRYSTALLOGRAPHIC STUDIES OF THE COLLAGEN-LIKE POLYPEPTIDE [(PRO-HYP-GLY)10)]3 : IMPLICATION FOR COLLAGEN STABILITY
No full textX-RAY DIFFRACTIVE QUALITY OF (PPG)10 CRYSTALS GROWN IN FOUR DIFFERENT CRYSTALLIZATION ENVIRONMENTS
No full textCrystal structure of the collagen-like polypeptide with repeating sequence Pro-Hyp-Gly: implications for collagen hydration
No full textCharacterization of collagen-like heterotrimers: implications for triple-helix stability.
No full textPE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
Full text linkTo the PE_PGRS protein subfamily belongs a group of surface-exposed mycobacterial antigens that in Mycobacterium tuberculosis (Mtb) H37Rv accounts to more than 65 genes, 51 of which are thought to express a functional protein. PE_PGRS proteins share a conserved structural architecture with three main domains: the N-terminal PE domain; the PGRS domain, that can vary in sequence and size and is characterized by the presence of multiple GGA-GGX amino acid repeats; the highly conserved sequence containing the GRPLI motif that links the PE and PGRS domains; the unique C-terminus end that can vary in size from few to up to ≈ 300 amino acids. pe_pgrs genes emerged in slow-growing mycobacteria and expanded and diversified in MTBC and few other pathogenic mycobacteria. Interestingly, despite sequence homology and apparent redundancy, PE_PGRS proteins seem to have evolved a peculiar function. In this review, we summarize the actual knowledge on this elusive protein family in terms of evolution, structure, and function, focusing on the role of PE_PGRS in TB pathogenesis. We provide an original hypothesis on the role of the PE domain and propose a structural model for the polymorphic PGRS domain that might explain how so similar proteins can have different physiological functions
Imino acids and collagen triple helix stability: characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats
No full textThe analysis of factors contributing to the stability of proteins is a subject of intense debate. Particularly challenging is the study of structural proteins, since their function is their structure. Among these is collagen, the key structural component of bones, skin, cartilage, tendons, and other connecting tissues. It is well established that the collagen triple helix is characterized by the presence of hydroxyproline, whose content modulates triple helix thermal stability according to the requirement of the host organism. Because of the complexity and the fibrous nature of collagen, data on the stability and structure of this protein have been mainly obtained by the use of collagen-like polypeptides. On the basis of CD characterization of collagen-like polypeptides we here show that the presence of Hyp at the X position of repeating triplets Hyp-Hyp-Gly stabilizes the triple helix significantly. This extra-stabilization has been ascribed, by using molecular modeling, to the formation of a hydrogen bond between Hyp residues belonging to the X and the Y positions of adjacent chains. This communication also provides a comprehensive interpretation of the ensemble of available data on polypeptides containing proline derivatives
CRYSTALLIZATION OF THE COLLAGEN-LIKE POLYPEPTIDE (PPG)10 ABOARD THE INTERNATIONAL SPACE STATION.2. COMPARISON OF CRYSTAL QUALITY BY X-RAY DIFFRACTION
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