1w3y

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[[Category: peptidoglycan-anchor]]
[[Category: peptidoglycan-anchor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:41:48 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:24:25 2007''

Revision as of 14:19, 30 October 2007


1w3y, resolution 1.65Å

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CRYSTAL STRUCTURE OF S. PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH PALMITOYL-VITAMIN C

Overview

Hyaluronidases are enzymes that degrade hyaluronan, an important component, of the extracellular matrix. The mammalian hyaluronidases are considered, to be involved in many (patho)physiological processes like fertilization, tumor growth, and metastasis. Bacterial hyaluronidases, also termed, hyaluronate lyases, contribute to the spreading of microorganisms in, tissues. Such roles for hyaluronidases suggest that inhibitors could be, useful pharmacological tools. Potent and selective inhibitors are not, known to date, although L-ascorbic acid has been reported to be a weak, inhibitor of Streptococcus pneumoniae hyaluronate lyase (SpnHL). The x-ray, structure of SpnHL complexed with L-ascorbic acid has been elucidated, suggesting that additional hydrophobic interactions might increase, ... [(full description)]

About this Structure

1W3Y is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with XYL, SO4 and PVC as [ligands]. Active as [Hyaluronate lyase], with EC number [4.2.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

L-Ascorbic acid 6-hexadecanoate, a potent hyaluronidase inhibitor. X-ray structure and molecular modeling of enzyme-inhibitor complexes., Botzki A, Rigden DJ, Braun S, Nukui M, Salmen S, Hoechstetter J, Bernhardt G, Dove S, Jedrzejas MJ, Buschauer A, J Biol Chem. 2004 Oct 29;279(44):45990-7. Epub 2004 Aug 18. PMID:15322107

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