1ix5: Difference between revisions

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[[Image:1ix5.jpg|left|200px]]<br /><applet load="1ix5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ix5.jpg|left|200px]]<br /><applet load="1ix5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ix5" />

'''Solution structure of the Methanococcus thermolithotrophicus FKBP'''<br />

==Overview==

Here we report the solution structure of an archaeal FK506-binding protein, (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus, (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and, chaperone-like activities, to reveal the structural basis for the dual, function. In addition to a typical PPIase domain, a newly identified, domain is formed in the flap loop by a 48-residue insert that is required, for the chaperone-like activity. The new domain, called IF domain (the, Insert in the Flap), is a novel-folding motif and exposes a hydrophobic, surface, which we consider to play an important role in the chaperone-like, activity.

Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity.

==About this Structure==

1IX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].

1IX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].

==Reference==

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[[Category: ppiase]]

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@@ Line 1: / Line 1: @@
-[[Image:1ix5.jpg|left|200px]]<br /><applet load="1ix5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ix5.jpg|left|200px]]<br /><applet load="1ix5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ix5" />
 '''Solution structure of the Methanococcus thermolithotrophicus FKBP'''<br />
 ==Overview==
-Here we report the solution structure of an archaeal FK506-binding protein, (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus, (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and, chaperone-like activities, to reveal the structural basis for the dual, function. In addition to a typical PPIase domain, a newly identified, domain is formed in the flap loop by a 48-residue insert that is required, for the chaperone-like activity. The new domain, called IF domain (the, Insert in the Flap), is a novel-folding motif and exposes a hydrophobic, surface, which we consider to play an important role in the chaperone-like, activity.
+Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity.
 ==About this Structure==
-IX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
+IX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: ppiase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:44:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:35 2008''