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| {{STRUCTURE_1yal| PDB=1yal | SCENE= }} | | {{STRUCTURE_1yal| PDB=1yal | SCENE= }} |
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| '''CARICA PAPAYA CHYMOPAPAIN AT 1.7 ANGSTROMS RESOLUTION'''
| | ===CARICA PAPAYA CHYMOPAPAIN AT 1.7 ANGSTROMS RESOLUTION=== |
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| ==Overview==
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| The X-ray structure of chymopapain, a cysteine proteinase isolated from the latex of the fruits of Carica papaya L., has been determined by molecular replacement methods and refined to a conventional R factor of 0.19 for all observed reflections in the range from 9.5 to 1.7 A resolution. The crystals used in this study contained a unique molecular species of chymopapain with two moles of thiomethyl attached to the two free cysteines per mole of enzyme. A comparison is made with the other known papaya proteinase X-ray structures: papain, caricain, and glycyl endopeptidase. Their backbone conformations are extremely similar except for two loop regions. Both regions are located at the surface of the protein and far away of the active site cleft. In each X-ray structure the same water network was found at the interface between the two domains of the enzyme. A close examination of the active site groove showed that the specificity restrictions dictated by the S2 subsite did not differ significantly among the four proteinases. | | The line below this paragraph, {{ABSTRACT_PUBMED_8973203}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8973203 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8973203}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Thiol protease]] | | [[Category: Thiol protease]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:04:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:32:58 2008'' |