1tia: Difference between revisions

Line 1:

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

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

caption="1tia, resolution 2.1Å" />

'''AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES'''<br />

==Overview==

The stability of globular proteins arises largely from the burial of, non-polar amino acids in their interior. These residues are efficiently, packed to eliminate energetically unfavorable cavities. Contrary to these, observations, high resolution X-ray crystallographic analyses of four, homologous lipases from filamentous fungi reveal an alpha/beta fold which, contains a buried conserved constellation of charged and polar side chains, with associated cavities containing ordered water molecules. It is, possible that this structural arrangement plays an important role in, interfacial catalysis.

The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis.

==About this Structure==

1TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TIA OCA].

1TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIA OCA].

==Reference==

Line 15:

[[Category: Triacylglycerol lipase]]

[[Category: Derewenda, U.]]

[[Category: Derewenda, Z.S.]]

[[Category: Derewenda, Z S.]]

[[Category: Swenson, L.]]

[[Category: Wei, Y.]]

Line 21:

[[Category: hydrolase(carboxylic esterase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 03:17:~~15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:47 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tia.gif|left|200px]]<br /><applet load="1tia" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tia.gif|left|200px]]<br /><applet load="1tia" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tia, resolution 2.1&Aring;" />
 '''AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF FUNGAL LIPASES'''<br />
 ==Overview==
-The stability of globular proteins arises largely from the burial of, non-polar amino acids in their interior. These residues are efficiently, packed to eliminate energetically unfavorable cavities. Contrary to these, observations, high resolution X-ray crystallographic analyses of four, homologous lipases from filamentous fungi reveal an alpha/beta fold which, contains a buried conserved constellation of charged and polar side chains, with associated cavities containing ordered water molecules. It is, possible that this structural arrangement plays an important role in, interfacial catalysis.
+The stability of globular proteins arises largely from the burial of non-polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X-ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an alpha/beta fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis.
 ==About this Structure==
-TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TIA OCA].
+TIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_camemberti Penicillium camemberti]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIA OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Triacylglycerol lipase]]
 [[Category: Derewenda, U.]]
-[[Category: Derewenda, Z.S.]]
+[[Category: Derewenda, Z S.]]
 [[Category: Swenson, L.]]
 [[Category: Wei, Y.]]
@@ Line 21: / Line 21: @@
 [[Category: hydrolase(carboxylic esterase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:17:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:47 2008''