Sandbox UNLPam 7

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(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...)
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==Your Heading Here (maybe something like 'Structure')==
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page '''Sandbox UNLPam 7'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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The crystal structure of the GH78 family a-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 A °
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is
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preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This
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KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures.
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Nevertheless, the enzyme displays a-rhamnosidase activity when assayed in vitro, suggesting that the additional structural
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domains found in the related enzymes are dispensible for function.
== Function ==
== Function ==

Revision as of 12:43, 9 December 2015

Your Heading Here (maybe something like 'Structure')

Caption for this structure

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References

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