1GXX

Solution structure of lysozyme at low and high pressure

Summary for 1GXX

• Entry DOI: 10.2210/pdb1gxx/pdb
• Related: 132L 193L 194L 1A2Y 1AKI 1AT5 1AT6 1AZF 1B0D 1B2K 1BGI 1BHZ 1BVK 1BVX 1BWH 1BWI 1BWJ 1C08 1C10 1DPW 1DPX 1DQJ 1E8L 1F0W 1F10 1F3J 1FDL 1FLQ 1FLU 1FLW 1FLY 1FN5 1G7H 1G7I 1G7J 1G7L 1G7M 1GPQ 1GWD 1GXV 1H6M 1H87 1HC0 1HEL 1HEM 1HEN 1HEO 1HEP 1HEQ 1HER 1HEW 1HF4 1HSW 1HSX 1IC4 1IC5 1IC7 1IEE 1IO5 1IOQ 1IOR 1IOS 1IOT 1IR7 1IR8 1IR9 1JA2 1JA4 1JA6 1JA7 1JIS 1JIT 1JIY 1JJ0 1JJ1 1JJ3 1JPO 1JTO 1KIP 1KIQ 1KIR 1KXW 1KXX 1KXY 1LCN 1LKR 1LKS 1LMA 1LPI 1LSA 1LSB 1LSC 1LSD 1LSE 1LSF 1LSG 1LSM 1LSN 1LSY 1LSZ 1LYO 1LYS 1LYZ 1LZ8 1LZ9 1LZA 1LZB 1LZC 1LZD 1LZE 1LZG 1LZH 1LZN 1LZT 1MEL 1MLC 1QIO 1QTK 1RCM 1RFP 1UCO 1UIA 1UIB 1UIC 1UID 1UIE 1UIF 1UIG 1UIH 1VFB 1XEI 1XEJ 1XEK 2HFM 2IFF 2LYM 2LYO 2LYZ 2LZH 2LZT 3HFL 3HFM 3LYM 3LYO 3LYT 3LYZ 3LZT 4LYM 4LYO 4LYT 4LYZ 4LZT 5LYM 5LYT 5LYZ 6LYT 6LYZ 7LYZ 8LYZ
• Descriptor: LYSOZYME C (2 entities in total)
• Functional Keywords: hydrolase, saccharide degradation, glycosidase, bacteriolytic enzyme, allergen, egg-white
• Biological source: GALLUS GALLUS (CHICKEN)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Refaee, M.,Akasaka, K.,Williamson, M. (deposition date: 2002-04-15, release date: 2003-03-27, Last modification date: 2011-07-13)

Primary citation

Refaee, M.,Tezuka, T.,Akasaka, K.,Williamson, M.
Pressure-Dependent Changes in the Solution Structure of Hen Egg-White Lysozyme
J.Mol.Biol., 327:857-, 2003

PubMed Abstract: The "rules" governing protein structure and stability are still poorly understood. Important clues have come from proteins that operate under extreme conditions, because these clarify the physical constraints on proteins. One obvious extreme is pressure, but so far little is known of the behavior of proteins under pressure, largely for technical reasons. We have therefore developed new methodology for calculating structure change in solution with pressure, using NMR chemical shift changes, and we report the change in structure of lysozyme on going from 30 bar to 2000 bar, this being the first solution structure of a globular protein under pressure. The alpha-helical domain is compressed by approximately 1%, due to tighter packing between helices. The interdomain region is also compressed. By contrast, the beta-sheet domain displays very little overall compression, but undergoes more structural distortion than the alpha-domain. The largest volume changes tend to occur close to hydrated cavities. Because isothermal compressibility is related to volume fluctuation, this suggests that buried water molecules play an important role in conformational fluctuation at normal pressures, and are implicated as the nucleation sites for structural changes leading to pressure denaturation or channel opening.

PubMed: 12654268
DOI: 10.1016/S0022-2836(03)00209-2

Experimental method

SOLUTION NMR