1uh9
From Proteopedia
(New page: 200px<br /><applet load="1uh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uh9, resolution 2.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:1uh9.jpg|left|200px]]<br /><applet load="1uh9" size=" | + | [[Image:1uh9.jpg|left|200px]]<br /><applet load="1uh9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uh9, resolution 2.0Å" /> | caption="1uh9, resolution 2.0Å" /> | ||
'''Crystal structure of rhizopuspepsin at pH 7.0'''<br /> | '''Crystal structure of rhizopuspepsin at pH 7.0'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of rhizopuspepsin has been determined at three | + | The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range. |
==About this Structure== | ==About this Structure== | ||
| - | 1UH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_microsporus_var._chinensis Rhizopus microsporus var. chinensis]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http:// | + | 1UH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_microsporus_var._chinensis Rhizopus microsporus var. chinensis]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UH9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhizopus microsporus var. chinensis]] | [[Category: Rhizopus microsporus var. chinensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Prasad, B | + | [[Category: Prasad, B V.L S.]] |
[[Category: Suguna, K.]] | [[Category: Suguna, K.]] | ||
[[Category: aspartic proteinase]] | [[Category: aspartic proteinase]] | ||
[[Category: pepsin]] | [[Category: pepsin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:28 2008'' |
Revision as of 13:24, 21 February 2008
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Crystal structure of rhizopuspepsin at pH 7.0
Overview
The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range.
About this Structure
1UH9 is a Single protein structure of sequence from Rhizopus microsporus var. chinensis. Active as Hydrolase, with EC number 3.4.23.18, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30 Full crystallographic information is available from OCA.
Reference
Effect of pH on the structure of rhizopuspepsin., Prasad BV, Suguna K, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1755-61. Epub 2003, Sep 19. PMID:14501114
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