179l - Revision history

OCA: Replacing page with 'REMOVED: The PDB entry 179l was removed.'

OCA — Fri, 11 Jul 2008 09:54:01 GMT

Replacing page with 'REMOVED: The PDB entry 179l was removed.'

←Older revision		Revision as of 09:54, 11 July 2008
Line 1:		Line 1:
-	~~{{Seed}}~~	+	REMOVED: The PDB entry 179l was removed.
-	~~[[Image~~:~~179l.png\|left\|200px]]~~	+
-		+
-	~~<!--~~	+
-	The ~~line below this paragraph, containing "STRUCTURE_179l", creates the "Structure Box" on the page.~~	+
-	~~You may change the~~ PDB ~~parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	~~-->~~	+
-	~~{{STRUCTURE_179l\| PDB=~~179l ~~\| SCENE= }}~~	+
-		+
-	~~===Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME===~~	+
-		+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_7616572}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at http://www~~.~~pubmed.gov), where 7616572 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_7616572}}~~	+
-		+
-	~~==About this Structure==~~	+
-	179L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].	+
-		+
-	~~==Reference==~~	+
-	Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7616572 7616572]	+
-	~~[[Category: Enterobacteria phage t4]]~~	+
-	~~[[Category: Lysozyme]]~~	+
-	~~[[Category: Single protein]]~~	+
-	~~[[Category: Matsumura, M.]]~~	+
-	~~[[Category: Matthews, B W.]]~~	+
-	~~[[Category: Weaver, L.]]~~	+
-	~~[[Category: Zhang, X J.]]~~	+
-		+
-	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:37:02 2008''~~	+

OCA at 12:37, 30 June 2008

OCA — Mon, 30 Jun 2008 12:37:09 GMT

←Older revision		Revision as of 12:37, 30 June 2008
Line 1:		Line 1:
-	[[Image:179l.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:179l.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_179l\| PDB=179l \| SCENE= }}		{{STRUCTURE_179l\| PDB=179l \| SCENE= }}

-	~~'''~~Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME~~'''~~	+	===Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME===


-	~~==Overview==~~	+	<!--
-	~~The structures of various mutants of T4 lysozyme have been determined in 25 non~~-isomorphous crystal forms. This provides an unusually diverse data base to compare the structures and dynamics of a closely related set of proteins in different crystal packing environments. In general, the more tightly packed crystals diffract better than those that are highly hydrated although the wild-~~type crystal form is an exception.~~ The ~~ability of the protein to form a relatively open but stable lattice may help explain why many of the mutants crystallize in~~ this ~~form. In different crystalline environments~~, the ~~lysozyme molecules associate with 2-fold, 3-fold, 4-fold, and 5-fold symmetry, as well as with various types of screw associations. A "back-~~to~~-back" dimeric association, and a "head-to-tail" 2~~(1) screw association, are especially common, each occurring in more than half a dozen crystal forms. The 4-fold and 5-fold modes of association are closely related and provide an example of quasi-equivalent association as ~~envisaged by Caspar and Klug~~. ~~In different crystal environments the lysozyme molecules display a range of over 50 degrees in the hinge-bending angle between the amino and carboxy-terminal domains~~. ~~Large variations in the hinge-bending angle are observed not only for lysozymes with mutations in the hinge region~~, ~~but for molecules with mutations far from this site. This suggests that hinge-bending~~ is ~~an intrinsic property of~~ the ~~lysozyme molecule and is not an artifact due to mutation~~. ~~As the hinge~~-~~bending angle increases about 15 degrees beyond that seen in wild~~-type there is a distinct conformations change in the side-chains of five residues in the hinge-bending region. Changes in the backbone are localized near residues 13, 59 and 80, but do not include significant changes in (phi, psi). Comparison of the different structures indicates that crystal contacts perturb the backbone structure of the protein by 0.2 to 0.5 A. These perturbations are of the same magnitude for helices and beta-sheet strands, suggesting that protein structures can be defined and maintained equally well by hydrogen-bonding (i.e. strand-strand) or by non-hydrogen-bonding (i.e. helix-helix) interactions. The discrepancies between the lysozyme structures in different crystallographic environments are in line with other comparisons of independently determined protein crystal structures. They suggest that protein structures in general are subject to low energy changes in conformation of 0.2 to 0.5 A.(ABSTRACT TRUNCATED AT 400 WORDS)	+	The line below this paragraph, {{ABSTRACT_PUBMED_7616572}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 7616572 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_7616572}}

	==About this Structure==		==About this Structure==
Line 27:		Line 31:
	[[Category: Weaver, L.]]		[[Category: Weaver, L.]]
	[[Category: Zhang, X J.]]		[[Category: Zhang, X J.]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Jun ~~5 09~~:53:05 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:37:02 2008''

OCA at 06:53, 5 June 2008

OCA — Thu, 05 Jun 2008 06:53:07 GMT

←Older revision		Revision as of 06:53, 5 June 2008
Line 9:		Line 9:
	{{STRUCTURE_179l\| PDB=179l \| SCENE= }}		{{STRUCTURE_179l\| PDB=179l \| SCENE= }}

-	'''~~PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN~~ 25 ~~CRYSTAL FORMS OF~~ T4 LYSOZYME'''	+	'''Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME'''


Line 27:		Line 27:
	[[Category: Weaver, L.]]		[[Category: Weaver, L.]]
	[[Category: Zhang, X J.]]		[[Category: Zhang, X J.]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 09:33:41 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 5 09:53:05 2008''

OCA at 06:33, 2 May 2008

OCA — Fri, 02 May 2008 06:33:41 GMT

←Older revision		Revision as of 06:33, 2 May 2008
Line 1:		Line 1:
	[[Image:179l.gif\|left\|200px]]		[[Image:179l.gif\|left\|200px]]

-	{{Structure	+	<!--
-	\|PDB~~= 179l \|SIZE=350\|CAPTION= <~~scene ~~name='initialview01'>179l</scene>~~, ~~resolution 2~~.~~7Å~~	+	The line below this paragraph, containing "STRUCTURE_179l", creates the "Structure Box" on the page.
-	~~\|SITE=~~	+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	~~\|LIGAND=~~	+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	~~\|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span~~>	+	or leave the SCENE parameter empty for the default display.
-	\|~~GENE~~=	+	-->
-	\|~~DOMAIN~~=	+	{{STRUCTURE_179l\| PDB=179l \| SCENE= }}
-	~~\|RELATEDENTRY=~~	+
-	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=179l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=179l OCA], [http://www.ebi.ac.uk/pdbsum/179l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=179l RCSB]</span>	+
-	}}	+

	'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''		'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''
Line 30:		Line 27:
	[[Category: Weaver, L.]]		[[Category: Weaver, L.]]
	[[Category: Zhang, X J.]]		[[Category: Zhang, X J.]]
-	~~[[Category: hydrolase (o-glycosyl)]]~~	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:33:41 2008''
-		+
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Mar 30 18~~:29:19 2008''	+

OCA at 15:29, 30 March 2008

OCA — Sun, 30 Mar 2008 15:29:20 GMT

←Older revision		Revision as of 15:29, 30 March 2008
Line 5:		Line 5:
	\|SITE=		\|SITE=
	\|LIGAND=		\|LIGAND=
-	\|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]	+	\|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
	\|GENE=		\|GENE=
		+	\|DOMAIN=
		+	\|RELATEDENTRY=
		+	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=179l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=179l OCA], [http://www.ebi.ac.uk/pdbsum/179l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=179l RCSB]</span>
	}}		}}

Line 16:		Line 19:

	==About this Structure==		==About this Structure==
-	179L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/~~Enterobacteria_phage_t2~~ Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].	+	179L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].

	==Reference==		==Reference==
	Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7616572 7616572]		Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7616572 7616572]
-	[[Category: Enterobacteria phage t2]]	+	[[Category: Enterobacteria phage t4]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Single protein]]		[[Category: Single protein]]
Line 29:		Line 32:
	[[Category: hydrolase (o-glycosyl)]]		[[Category: hydrolase (o-glycosyl)]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Mar ~~20 09~~:50:23 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:29:19 2008''

OCA at 07:50, 20 March 2008

OCA — Thu, 20 Mar 2008 07:50:23 GMT

←Older revision		Revision as of 07:50, 20 March 2008
Line 1:		Line 1:
-	[[Image:179l.gif\|left\|200px]]~~<br /><applet load~~="179l~~" size~~="350~~" color~~=~~"white" frame="true" align="right" spinBox~~=~~"true"~~	+	[[Image:179l.gif\|left\|200px]]
-	~~caption="~~179l, resolution 2.7Å" />	+
-	'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''~~<br />~~	+	{{Structure
		+	\|PDB= 179l \|SIZE=350\|CAPTION= <scene name='initialview01'>179l</scene>, resolution 2.7Å
		+	\|SITE=
		+	\|LIGAND=
		+	\|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
		+	\|GENE=
		+	}}
		+
		+	'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''
		+

	==Overview==		==Overview==
Line 7:		Line 16:

	==About this Structure==		==About this Structure==
-	179L is a [~~http://en.wikipedia.org/wiki/Single_protein~~ Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. ~~Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].	+	179L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].

	==Reference==		==Reference==
-	Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://~~ispc~~.~~weizmann~~.ac.~~il/~~/~~pmbin~~/~~getpm?pmid=~~7616572 7616572]	+	Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7616572 7616572]
	[[Category: Enterobacteria phage t2]]		[[Category: Enterobacteria phage t2]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
Line 20:		Line 29:
	[[Category: hydrolase (o-glycosyl)]]		[[Category: hydrolase (o-glycosyl)]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu ~~Feb 21 11~~:38:53 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:50:23 2008''

OCA at 09:38, 21 February 2008

OCA — Thu, 21 Feb 2008 09:38:54 GMT

←Older revision		Revision as of 09:38, 21 February 2008
Line 1:		Line 1:
-	[[Image:179l.gif\|left\|200px]]<br /><applet load="179l" size="~~450~~" color="white" frame="true" align="right" spinBox="true"	+	[[Image:179l.gif\|left\|200px]]<br /><applet load="179l" size="350" color="white" frame="true" align="right" spinBox="true"
	caption="179l, resolution 2.7Å" />		caption="179l, resolution 2.7Å" />
	'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''<br />		'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''<br />

	==Overview==		==Overview==
-	The structures of various mutants of T4 lysozyme have been determined in, 25 non-isomorphous crystal forms. This provides an unusually diverse data, base to compare the structures and dynamics of a closely related set of, proteins in different crystal packing environments. In general, the more, tightly packed crystals diffract better than those that are highly, hydrated although the wild-type crystal form is an exception. The ability, of the protein to form a relatively open but stable lattice may help, explain why many of the mutants crystallize in this form. In different, crystalline environments, the lysozyme molecules associate with 2-fold, 3-fold, 4-fold, and 5-fold symmetry, as well as with various types of, screw associations. A "back-to-back" dimeric association, and a, "head-to-tail" 2(1) screw association, are especially common, each, occurring in more than half a dozen crystal forms. The 4-fold and 5-fold, modes of association are closely related and provide an example of, quasi-equivalent association as envisaged by Caspar and Klug. In different, crystal environments the lysozyme molecules display a range of over 50, degrees in the hinge-bending angle between the amino and carboxy-terminal, domains. Large variations in the hinge-bending angle are observed not only, for lysozymes with mutations in the hinge region, but for molecules with, mutations far from this site. This suggests that hinge-bending is an, intrinsic property of the lysozyme molecule and is not an artifact due to, mutation. As the hinge-bending angle increases about 15 degrees beyond, that seen in wild-type there is a distinct conformations change in the, side-chains of five residues in the hinge-bending region. Changes in the, backbone are localized near residues 13, 59 and 80, but do not include, significant changes in (phi, psi). Comparison of the different structures, indicates that crystal contacts perturb the backbone structure of the, protein by 0.2 to 0.5 A. These perturbations are of the same magnitude for, helices and beta-sheet strands, suggesting that protein structures can be, defined and maintained equally well by hydrogen-bonding (i.e., strand-strand) or by non-hydrogen-bonding (i.e. helix-helix) interactions., The discrepancies between the lysozyme structures in different, crystallographic environments are in line with other comparisons of, independently determined protein crystal structures. They suggest that, protein structures in general are subject to low energy changes in, conformation of 0.2 to 0.5 A.(ABSTRACT TRUNCATED AT 400 WORDS)	+	The structures of various mutants of T4 lysozyme have been determined in 25 non-isomorphous crystal forms. This provides an unusually diverse data base to compare the structures and dynamics of a closely related set of proteins in different crystal packing environments. In general, the more tightly packed crystals diffract better than those that are highly hydrated although the wild-type crystal form is an exception. The ability of the protein to form a relatively open but stable lattice may help explain why many of the mutants crystallize in this form. In different crystalline environments, the lysozyme molecules associate with 2-fold, 3-fold, 4-fold, and 5-fold symmetry, as well as with various types of screw associations. A "back-to-back" dimeric association, and a "head-to-tail" 2(1) screw association, are especially common, each occurring in more than half a dozen crystal forms. The 4-fold and 5-fold modes of association are closely related and provide an example of quasi-equivalent association as envisaged by Caspar and Klug. In different crystal environments the lysozyme molecules display a range of over 50 degrees in the hinge-bending angle between the amino and carboxy-terminal domains. Large variations in the hinge-bending angle are observed not only for lysozymes with mutations in the hinge region, but for molecules with mutations far from this site. This suggests that hinge-bending is an intrinsic property of the lysozyme molecule and is not an artifact due to mutation. As the hinge-bending angle increases about 15 degrees beyond that seen in wild-type there is a distinct conformations change in the side-chains of five residues in the hinge-bending region. Changes in the backbone are localized near residues 13, 59 and 80, but do not include significant changes in (phi, psi). Comparison of the different structures indicates that crystal contacts perturb the backbone structure of the protein by 0.2 to 0.5 A. These perturbations are of the same magnitude for helices and beta-sheet strands, suggesting that protein structures can be defined and maintained equally well by hydrogen-bonding (i.e. strand-strand) or by non-hydrogen-bonding (i.e. helix-helix) interactions. The discrepancies between the lysozyme structures in different crystallographic environments are in line with other comparisons of independently determined protein crystal structures. They suggest that protein structures in general are subject to low energy changes in conformation of 0.2 to 0.5 A.(ABSTRACT TRUNCATED AT 400 WORDS)

	==About this Structure==		==About this Structure==
-	179L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].	+	179L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].

	==Reference==		==Reference==
Line 15:		Line 15:
	[[Category: Single protein]]		[[Category: Single protein]]
	[[Category: Matsumura, M.]]		[[Category: Matsumura, M.]]
-	[[Category: Matthews, B.W.]]	+	[[Category: Matthews, B W.]]
	[[Category: Weaver, L.]]		[[Category: Weaver, L.]]
-	[[Category: Zhang, X.J.]]	+	[[Category: Zhang, X J.]]
	[[Category: hydrolase (o-glycosyl)]]		[[Category: hydrolase (o-glycosyl)]]

-	''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 10~~:30:~~02 2007~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:38:53 2008''

OCA: New page: 200px
'''PROTEIN FLEXIBILITY A...
OCA — Tue, 20 Nov 2007 08:22:51 GMT

New page: 200px<br /><applet load="179l" size="450" color="white" frame="true" align="right" spinBox="true" caption="179l, resolution 2.7Å" /> '''PROTEIN FLEXIBILITY A...

New page
[[Image:179l.gif|left|200px]]<br /><applet load="179l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="179l, resolution 2.7Å" />
'''PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME'''<br />

==Overview==
The structures of various mutants of T4 lysozyme have been determined in, 25 non-isomorphous crystal forms. This provides an unusually diverse data, base to compare the structures and dynamics of a closely related set of, proteins in different crystal packing environments. In general, the more, tightly packed crystals diffract better than those that are highly, hydrated although the wild-type crystal form is an exception. The ability, of the protein to form a relatively open but stable lattice may help, explain why many of the mutants crystallize in this form. In different, crystalline environments, the lysozyme molecules associate with 2-fold, 3-fold, 4-fold, and 5-fold symmetry, as well as with various types of, screw associations. A "back-to-back" dimeric association, and a, "head-to-tail" 2(1) screw association, are especially common, each, occurring in more than half a dozen crystal forms. The 4-fold and 5-fold, modes of association are closely related and provide an example of, quasi-equivalent association as envisaged by Caspar and Klug. In different, crystal environments the lysozyme molecules display a range of over 50, degrees in the hinge-bending angle between the amino and carboxy-terminal, domains. Large variations in the hinge-bending angle are observed not only, for lysozymes with mutations in the hinge region, but for molecules with, mutations far from this site. This suggests that hinge-bending is an, intrinsic property of the lysozyme molecule and is not an artifact due to, mutation. As the hinge-bending angle increases about 15 degrees beyond, that seen in wild-type there is a distinct conformations change in the, side-chains of five residues in the hinge-bending region. Changes in the, backbone are localized near residues 13, 59 and 80, but do not include, significant changes in (phi, psi). Comparison of the different structures, indicates that crystal contacts perturb the backbone structure of the, protein by 0.2 to 0.5 A. These perturbations are of the same magnitude for, helices and beta-sheet strands, suggesting that protein structures can be, defined and maintained equally well by hydrogen-bonding (i.e., strand-strand) or by non-hydrogen-bonding (i.e. helix-helix) interactions., The discrepancies between the lysozyme structures in different, crystallographic environments are in line with other comparisons of, independently determined protein crystal structures. They suggest that, protein structures in general are subject to low energy changes in, conformation of 0.2 to 0.5 A.(ABSTRACT TRUNCATED AT 400 WORDS)

==About this Structure==
179L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=179L OCA].

==Reference==
Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme., Zhang XJ, Wozniak JA, Matthews BW, J Mol Biol. 1995 Jul 21;250(4):527-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7616572 7616572]
[[Category: Enterobacteria phage t2]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Matsumura, M.]]
[[Category: Matthews, B.W.]]
[[Category: Weaver, L.]]
[[Category: Zhang, X.J.]]
[[Category: hydrolase (o-glycosyl)]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:30:02 2007''