4git

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'''Unreleased structure'''
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{{STRUCTURE_4git| PDB=4git | SCENE= }}
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===Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber===
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The entry 4git is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]
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Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H.
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==About this Structure==
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[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA].
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Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber
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[[Category: Brevibacillus thermoruber]]
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[[Category: Endopeptidase La]]
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[[Category: Chang, Y Y.]]
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[[Category: Chen, Y D.]]
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[[Category: Hsu, C H.]]
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[[Category: Dna binding]]
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[[Category: Hydrolase]]

Revision as of 05:29, 12 September 2013

Template:STRUCTURE 4git

Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber

Function

[Q84FG5_9BACL] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]

About this Structure

4git is a 2 chain structure with sequence from Brevibacillus thermoruber. Full crystallographic information is available from OCA.

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OCA

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