1p92
From Proteopedia
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| - | [[Image:1p92.gif|left|200px]] | + | [[Image:1p92.gif|left|200px]] |
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| - | '''Crystal Structure of (H79A)DtxR''' | + | {{Structure |
| + | |PDB= 1p92 |SIZE=350|CAPTION= <scene name='initialview01'>1p92</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= DTXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1717 Corynebacterium diphtheriae]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of (H79A)DtxR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P92 is a [ | + | 1P92 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P92 OCA]. |
==Reference== | ==Reference== | ||
| - | Determinants of the SRC homology domain 3-like fold., D'Aquino JA, Ringe D, J Bacteriol. 2003 Jul;185(14):4081-6. PMID:[http:// | + | Determinants of the SRC homology domain 3-like fold., D'Aquino JA, Ringe D, J Bacteriol. 2003 Jul;185(14):4081-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837782 12837782] |
[[Category: Corynebacterium diphtheriae]] | [[Category: Corynebacterium diphtheriae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh3-like]] | [[Category: sh3-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:21:28 2008'' |
Revision as of 11:21, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | DTXR (Corynebacterium diphtheriae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of (H79A)DtxR
Overview
In eukaryotes, the Src homology domain 3 (SH3) is a very important motif in signal transduction. SH3 domains recognize poly-proline-rich peptides and are involved in protein-protein interactions. Until now, the existence of SH3 domains has not been demonstrated in prokaryotes. However, the structure of the C-terminal domain of DtxR clearly shows that the fold of this domain is very similar to that of the SH3 domain. In addition, there is evidence that the C-terminal domain of DtxR binds to poly-proline-rich regions. Other bacterial proteins have domains that are structurally similar to the SH3 domain but whose functions are unknown or differ from that of the SH3 domain. The observed similarities between the structures of the C-terminal domain of DtxR and the SH3 domain constitute a perfect system to gain insight into their function and information about their evolution. Our results show that the C-terminal domain of DtxR shares a number of conserved key hydrophobic positions not recognizable from sequence comparison that might be responsible for the integrity of the SH3-like fold. Structural alignment of an ensemble of such domains from unrelated proteins shows a common structural core that seems to be conserved despite the lack of sequence similarity. This core constitutes the minimal requirements of protein architecture for the SH3-like fold.
About this Structure
1P92 is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.
Reference
Determinants of the SRC homology domain 3-like fold., D'Aquino JA, Ringe D, J Bacteriol. 2003 Jul;185(14):4081-6. PMID:12837782
Page seeded by OCA on Thu Mar 20 13:21:28 2008
