2f1e

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(New page: 200px<br /><applet load="2f1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f1e" /> '''Solution structure of ApaG protein'''<br /> ...)
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'''Solution structure of ApaG protein'''<br />
'''Solution structure of ApaG protein'''<br />
==Overview==
==Overview==
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ApaG proteins are found in a wide variety of bacterial genomes but their, function is as yet unknown. Some eukaryotic proteins involved in, protein-protein interactions, such as the human polymerase, delta-interacting protein (PDIP38) and the F Box A (FBA) proteins, contain, ApaG homology domains. We have used NMR to determine the solution, structure of ApaG protein from the plant pathogen Xanthomonas axonopodis, pv. citri (ApaG(Xac)) with the aim to shed some light on its molecular, function. ApaG(Xac) is characterized by seven antiparallel beta strands, forming two beta sheets, one containing three strands (ABE) and the other, four strands (GFCC'). Relaxation measurements indicate that the protein, has a quite rigid structure. In spite of the presence of a putative GXGXXG, pyrophosphate binding motif ApaG(Xac) does not bind ATP or GTP, in vitro., On the other hand, ApaG(Xac) adopts a fibronectin type III (Fn3) fold, which is consistent with the hypothesis that it is involved in mediating, protein-protein interactions. The fact that the proteins of ApaG family do, not display significant sequence similarity with the Fn3 domains found in, other eukaryotic or bacterial proteins suggests that Fn3 domain may have, arisen earlier in evolution than previously estimated.
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ApaG proteins are found in a wide variety of bacterial genomes but their function is as yet unknown. Some eukaryotic proteins involved in protein-protein interactions, such as the human polymerase delta-interacting protein (PDIP38) and the F Box A (FBA) proteins, contain ApaG homology domains. We have used NMR to determine the solution structure of ApaG protein from the plant pathogen Xanthomonas axonopodis pv. citri (ApaG(Xac)) with the aim to shed some light on its molecular function. ApaG(Xac) is characterized by seven antiparallel beta strands forming two beta sheets, one containing three strands (ABE) and the other four strands (GFCC'). Relaxation measurements indicate that the protein has a quite rigid structure. In spite of the presence of a putative GXGXXG pyrophosphate binding motif ApaG(Xac) does not bind ATP or GTP, in vitro. On the other hand, ApaG(Xac) adopts a fibronectin type III (Fn3) fold, which is consistent with the hypothesis that it is involved in mediating protein-protein interactions. The fact that the proteins of ApaG family do not display significant sequence similarity with the Fn3 domains found in other eukaryotic or bacterial proteins suggests that Fn3 domain may have arisen earlier in evolution than previously estimated.
==About this Structure==
==About this Structure==
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2F1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_axonopodis_pv._citri Xanthomonas axonopodis pv. citri]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F1E OCA].
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2F1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_axonopodis_pv._citri Xanthomonas axonopodis pv. citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1E OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xanthomonas axonopodis pv. citri]]
[[Category: Xanthomonas axonopodis pv. citri]]
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[[Category: Cicero, D.O.]]
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[[Category: Cicero, D O.]]
[[Category: Contessa, G.]]
[[Category: Contessa, G.]]
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[[Category: Farah, C.S.]]
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[[Category: Farah, C S.]]
[[Category: Paci, M.]]
[[Category: Paci, M.]]
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[[Category: Pertinhez, T.A.]]
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[[Category: Pertinhez, T A.]]
[[Category: Spisni, A.]]
[[Category: Spisni, A.]]
[[Category: apag protein]]
[[Category: apag protein]]
[[Category: nmr]]
[[Category: nmr]]
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[[Category: xanthomonas axonopodis pv.citri]]
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[[Category: xanthomonas axonopodis pv citri]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:18:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:42 2008''

Revision as of 15:16, 21 February 2008


2f1e

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Solution structure of ApaG protein

Overview

ApaG proteins are found in a wide variety of bacterial genomes but their function is as yet unknown. Some eukaryotic proteins involved in protein-protein interactions, such as the human polymerase delta-interacting protein (PDIP38) and the F Box A (FBA) proteins, contain ApaG homology domains. We have used NMR to determine the solution structure of ApaG protein from the plant pathogen Xanthomonas axonopodis pv. citri (ApaG(Xac)) with the aim to shed some light on its molecular function. ApaG(Xac) is characterized by seven antiparallel beta strands forming two beta sheets, one containing three strands (ABE) and the other four strands (GFCC'). Relaxation measurements indicate that the protein has a quite rigid structure. In spite of the presence of a putative GXGXXG pyrophosphate binding motif ApaG(Xac) does not bind ATP or GTP, in vitro. On the other hand, ApaG(Xac) adopts a fibronectin type III (Fn3) fold, which is consistent with the hypothesis that it is involved in mediating protein-protein interactions. The fact that the proteins of ApaG family do not display significant sequence similarity with the Fn3 domains found in other eukaryotic or bacterial proteins suggests that Fn3 domain may have arisen earlier in evolution than previously estimated.

About this Structure

2F1E is a Single protein structure of sequence from Xanthomonas axonopodis pv. citri. Full crystallographic information is available from OCA.

Reference

Solution structure of ApaG from Xanthomonas axonopodis pv. citri reveals a fibronectin-3 fold., Cicero DO, Contessa GM, Pertinhez TA, Gallo M, Katsuyama AM, Paci M, Farah CS, Spisni A, Proteins. 2007 May 1;67(2):490-500. PMID:17256769

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