1gzj

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(New page: 200px<br /><applet load="1gzj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gzj, resolution 1.62&Aring;" /> '''STRUCTURE OF THERMOA...)
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caption="1gzj, resolution 1.62&Aring;" />
'''STRUCTURE OF THERMOASCUS AURANTIACUS FAMILY 5 ENDOGLUCANASE'''<br />
'''STRUCTURE OF THERMOASCUS AURANTIACUS FAMILY 5 ENDOGLUCANASE'''<br />
==Overview==
==Overview==
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The crystal structure of Thermoascus aurantiacus endoglucanase (Cel5A), a, family 5 glycoside hydrolase, has been determined to 1.62 A resolution by, multiple isomorphous replacement with anomalous scattering. It is the, first report of a structure in the subfamily to which Cel5A belongs. Cel5A, consists solely of a catalytic module with compact eight-fold beta/alpha, barrel architecture. The length of the tryptophan-rich substrate binding, groove suggests the presence of substrate binding subsites -4 to +3., Structural comparison shows that two glycines are completely conserved in, the family, in addition to the two catalytic glutamates and six other, conserved residues previously identified. Gly 44 in particular is part of, a type IV C-terminal helix capping motif, whose disruption is likely to, affect the position of an essential conserved arginine. One aromatic, residue (Trp 170 in Cel5A), not conserved in term of sequence, is, nonetheless spatially conserved in the substrate binding groove. Its role, might be to force the bend that occurs in the polysaccharide chain on, binding, thus favoring substrate distortion at subsite -1.
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The crystal structure of Thermoascus aurantiacus endoglucanase (Cel5A), a family 5 glycoside hydrolase, has been determined to 1.62 A resolution by multiple isomorphous replacement with anomalous scattering. It is the first report of a structure in the subfamily to which Cel5A belongs. Cel5A consists solely of a catalytic module with compact eight-fold beta/alpha barrel architecture. The length of the tryptophan-rich substrate binding groove suggests the presence of substrate binding subsites -4 to +3. Structural comparison shows that two glycines are completely conserved in the family, in addition to the two catalytic glutamates and six other conserved residues previously identified. Gly 44 in particular is part of a type IV C-terminal helix capping motif, whose disruption is likely to affect the position of an essential conserved arginine. One aromatic residue (Trp 170 in Cel5A), not conserved in term of sequence, is nonetheless spatially conserved in the substrate binding groove. Its role might be to force the bend that occurs in the polysaccharide chain on binding, thus favoring substrate distortion at subsite -1.
==About this Structure==
==About this Structure==
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1GZJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GZJ OCA].
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1GZJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZJ OCA].
==Reference==
==Reference==
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[[Category: Thermoascus aurantiacus]]
[[Category: Thermoascus aurantiacus]]
[[Category: Larsen, S.]]
[[Category: Larsen, S.]]
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[[Category: Leggio, L.Lo.]]
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[[Category: Leggio, L Lo.]]
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[[Category: Pickersgill, R.W.]]
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[[Category: Pickersgill, R W.]]
[[Category: family 5]]
[[Category: family 5]]
[[Category: glycoside hydrolase]]
[[Category: glycoside hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:01:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:44 2008''

Revision as of 10:55, 21 February 2008


1gzj, resolution 1.62Å

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STRUCTURE OF THERMOASCUS AURANTIACUS FAMILY 5 ENDOGLUCANASE

Overview

The crystal structure of Thermoascus aurantiacus endoglucanase (Cel5A), a family 5 glycoside hydrolase, has been determined to 1.62 A resolution by multiple isomorphous replacement with anomalous scattering. It is the first report of a structure in the subfamily to which Cel5A belongs. Cel5A consists solely of a catalytic module with compact eight-fold beta/alpha barrel architecture. The length of the tryptophan-rich substrate binding groove suggests the presence of substrate binding subsites -4 to +3. Structural comparison shows that two glycines are completely conserved in the family, in addition to the two catalytic glutamates and six other conserved residues previously identified. Gly 44 in particular is part of a type IV C-terminal helix capping motif, whose disruption is likely to affect the position of an essential conserved arginine. One aromatic residue (Trp 170 in Cel5A), not conserved in term of sequence, is nonetheless spatially conserved in the substrate binding groove. Its role might be to force the bend that occurs in the polysaccharide chain on binding, thus favoring substrate distortion at subsite -1.

About this Structure

1GZJ is a Single protein structure of sequence from Thermoascus aurantiacus. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.

Reference

The 1.62 A structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5., Lo Leggio L, Larsen S, FEBS Lett. 2002 Jul 17;523(1-3):103-8. PMID:12123813

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